Atlas of Genetics and Cytogenetics in Oncology and Haematology


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Abstract

Abstract Stathmin 1 (STMN1) is a microtubule destabilizer protein with an important role in cell cycle progression, cell proliferation, migration and survival. The present review on STMN1 contains data on DNA/RNA, on the protein encoded and where the gene is implicated.

STMN1 (stathmin 1)

Identity

Other namesC1orf215
LAP18
Lag
OP18
PP17
PP19
PR22
SMN
HGNC (Hugo) STMN1
LocusID (NCBI) 3925
Location 1p36.11
Location_base_pair Starts at 26210677 and ends at 26232993 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

Note The entire STMN1 gene is about 22.8 kb and contains 5 exons (start: 26210672 bp and end: 26233482; orientation: minus strand). The STMN1 gene encodes 2 isoforms, A and B. Isoform A contains 3 transcript variants that differ in the 5' UTR and have an alternate terminal exon, compared to isoform B, resulting in a shorter and distinct C-terminus. The isoform B represents the longest transcript variant.

Protein

 
  Figure 1. Representation of primary structure of Stathmin 1 protein. The catastrophe promotion region (aa 1 - 99) and the four serine phosphorylation sites (S16, S25, S38 and S63) at the N-terminal, and the tubulin binding domain (aa 25 - 149) at the C-terminal are illustrated in the figure. Reproduced with permission of the editor-in-chief of BMB reports from Machado-Neto et al., 2014b.
Description Stathmin 1 belongs to the Stathmin protein family, which is characterized by the presence of a Stathmin-like domain (also known as tubulin-binding domain) that participates in interactions/sequestering of alpha/beta-tubulin heterodimers (Figure 1).
Expression Ubiquitous. Stathmin 1 is highly expressed during embryonic development. In adult cells, it is expressed during cell proliferation, and in nervous tissue and testis (revised in Curmi et al., 1999).
 
  Figure 2. Intracellular localization of Stathmin 1 protein in HeLa cells. Confocal analysis of HeLa cells displaying Stathmin 1 (green), Actin (red) and DAPI (blue) staining; MERGE shows the overlapped images. Scale bar: 10 μm. Note the predominant cytoplasmic localization of Stathmin 1. Anti-Stathmin 1 (OP18; sc-55531) was from Santa Cruz Biotechnology, (Santa Cruz, CA, USA), Phalloidin (A12379) and DAPI (P-36931) were from Invitrogen (Carlsbad, CA, USA). Personal data.
Localisation Stathmin 1 is predominantly found in the cytoplasm (Figure 2).
 
  Figure 3. Stathmin 1 signaling. Stathmin 1 may be phosphorylated on serine sites by cyclin-dependent kinases (CDKs), mitogen-activated protein kinases (MAPKs), phosphoinositide 3-kinase (PI3K), aurora kinase B (AURKB), protein kinase A (PKA), and Ca2+/calmodulin-dependent protein kinases (CamKs), leading to microtubule stability. On the other hand, Stathmin 1 may be dephosphorylated by protein phosphatase 1 (PP1), protein phosphatase 2A (PP2A) and protein phosphatase 2B (PP2B), resulting in microtubule instability. Abbreviations: TKR: tyrosine kinase receptor; P: phosphorylation; Ac: acetylation. This figure was performed using Servier Medical Art tools (http://www.servier.com/Powerpoint-image-bank).
Function Stathmin 1 is a phosphoprotein that participates in microtubule catastrophe and/or in the sequestering of alpha/beta-tubulin heterodimers, regulates microtubule dynamics, cell cycle progression, proliferation, motility and survival (Curmi et al., 1999; Belletti and Baldassarre, 2011). The main mechanism of regulation of Stathmin 1 activity on based in its phophorylated and unphosphorylated status at serine sites (residues 16, 25, 38 and 68). Stathmin 1 phosphorylation at serine 16 and/or 63 reduces the affinity between Stathmin 1 and alpha/beta-tubulin heterodimers. The proteins that are able to phosphorylate Stathmin 1 at serine 16 and/or 63 are: aurora kinase B, protein kinase A (PKA), P21 protein (Cdc42/Rac)-activated kinase (PAK1) and Ca2+/calmodulin-dependent protein kinases (CamKs). Serine 25 and/or 38 may be phosphorylated by cyclin-dependent kinases (CDKs), mitogen-activated protein kinases (MAPKs) and phosphoinositide 3-kinase (PI3K) (Belletti and Baldassarre, 2011). Phosphatase proteins that are able to dephosphorylate Stathmin 1 includes: protein phosphatase 1 (PP1), protein phosphatase 2A (PP2A) and protein phosphatase 2B (PP2B) (Guy et al., 1992; Tournebize et al., 1997; Mistry et al., 1998) (Figure 3).
Homology Stathmin 1 shares high homology with the other members of the Stathmin protein family including Stathmin-like 2 (also named SCG10), Stathmin-like 3 (also named SCLIP) and Stathmin-like 4 (also named RB3). Stathmin 1 also shares high homology among different species (Table 1).
 
  Table 1. Comparative identity of human STMN1 with other species. Source: HomoloGene.

Mutations

Note Recurrent mutations in the STMN1 gene are rare, 10 missense, 8 nonsense, 1 nonstop extension and 3 coding silent mutations are reported at COSMIC (catalogue of somatic mutations in cancer; COSMIC). In human esophageal adenocarcinoma, STMN1 Q18E mutation was identified and presented transformation potential in vitro and in vivo in NIH3T3 cells (Misek et al., 2002). Studies performed in leukemia cells indicate that the Q18E mutation results in Stathmin 1 hyperactivity and contributes to chromosomal instability (Holmfeldt et al., 2006).

Implicated in

Entity Various cancers
Note The role and clinical impact of Stathmin 1 has been extensively addressed in many types of human cancers. In general, the increased expression of Stathmin 1 is found in many cancers and confers a poor prognosis (revised in Belletti and Baldassarre, 2011 and Rana et al., 2008). Using cancer cell line models, several groups have demonstrated that Stathmin 1 inhibition may partially reverse the malignant phenotype.
  
Entity Hematopoietic neoplasms
Note Stathmin 1 was initially identified by proteomics analysis of HL60 leukemia cells (Feuerstein and Cooper, 1983). In primary acute leukemia and lymphoma samples, and leukemia cell lines, several independent groups have showed that Stathmin 1 is highly expressed (Hanash et al., 1988; Melhem et al., 1991; Melhem et al., 1997; Roos et al., 1993; Machado-Neto et al., 2014a; Brattsand et al., 1993); however its impact on survival outcome remains unknown. A recent study of immunophenotypic and molecular features of a large series of follicular lymphomas indicated that Stathmin 1 represents an useful novel diagnostic marker for these diseases (Marafioti et al., 2013). Importantly, Stathmin 1 silencing resulted in marked inhibition of tumorigenicity, proliferation and clonogenicity in leukemia cell lines (K562, U937 and Namalwa cells) (Machado-Neto et al., 2014a; Jeha et al., 1996; Iancu et al., 2001).
In a study that focused on the identification of biomarkers of human aging and aging-related diseases, Stathmin 1 was found upregulated in plasma samples from myelodysplastic patients (Jiang et al., 2008). Recently, increased levels of Stathmin 1 were reported in bone marrow and CD34+ cells from high-risk myelodysplastic syndromes patients and during disease progression (Machado-Neto et al., 2014a). Notably, higher Stathmin 1 expression was associated with high-risk disease and higher bone marrow blasts percentage (Machado-Neto et al., 2014a), but did not impacted survival.
Stathmin 1 was also identified as one of the 15 most relevant genes for determining the outcome in myeloma multiple patients by microarray approach (Decaux et al., 2008).
  
Entity Breast cancer
Note Using Western blot analysis, Brattsand (Brattsand, 2000) reported that Stathmin 1 expression positively correlated with proliferation status and aggressiveness in a panel of 151 primary breast carcinoma samples. Similar results were found by Curmi and colleagues (Curmi et al., 2000), who also reported that Stathmin 1 overexpression correlated with loss of steroid receptors, histopathological grade III and mitotic index. Importantly, Stathmin 1 expression was indicated as a potential tool for predicting the outcome of breast cancer patients with lymph node metastasis and its expression was increased in the group with poor prognosis (Oishi et al., 2007). By multivariate analysis, high Stathmin 1 expression predicted reduced disease-free survival (Saal et al., 2007; Golouh et al., 2008; Baquero et al., 2012) and overall survival (Baquero et al., 2012). Decreased Stathmin 1 phosphorylation at serine 16 (an inhibitory site) correlated with the more metastatic phenotype in breast cancers cell lines and primary tumors (Li et al., 2011). Using breast cancer cell lines and gene therapy tools, Stathmin 1 inhibition, by adenovirus-mediated gene transfer of anti-Stathmin 1 ribozyme, resulted in a dose-dependent inhibition of proliferation, apoptosis induction and had an additive effect together low concentration of taxol treatment in vitro and in vivo (Miceli et al., 2013).
  
Entity Ovarian cancer
Note Stathmin 1 overexpression has been described in ovarian cancer patients (Alaiya et al., 1997; Price et al., 2000). Wei and colleagues (Wei et al., 2008) observed that Stathmin 1 was expressed in all ovarian cancer samples analyzed and higher levels were observed in the metastatic tumors and negatively impacted survival by univariate analysis. In agreement, Stathmin 1 overexpression was found in primary high-grade serous ovarian carcinomas and ovarian cancer cell lines (Karst et al., 2011). High levels of Stathmin 1 predicted an unfavorable prognosis in ovarian cancer patients under paclitaxel and/or platinum therapy (Su et al., 2009; Aoki et al., 2009) also by univariate analysis. In p53 mutated ovarian cancer cell lines, Stathmin 1 silencing caused cell cycle arrest and apoptosis in vivo and in vivo (Sonego et al., 2013).
  
Entity Head and neck cancer
Note Using proteomics approach, Stathmin 1 was found to be differently expressed in oral squamous-cell carcinoma and laryngeal squamous-cell carcinoma (Koike et al., 2005; Sewell et al., 2007). Stathmin 1 expression was also found to be significantly increased in oral squamous-cell carcinoma cell lines and primary tumors and its high expression correlated with advanced stages of the disease and poor disease-free survival by univariate analysis (Kouzu et al., 2006). In head-neck squamous-cell carcinoma, Stathmin 1 was expressed at low levels (76% cases) and did not impact recurrence (Canzonieri et al., 2012). Cheng and colleagues (Cheng et al., 2008) identified an upregulation of Stathmin 1 in primary nasopharyngeal carcinoma and its expression was associated with recurrence and advanced stages of the disease. In agreement, Hsu and colleagues (Hsu et al., 2014) reported that Stathmin 1 was overexpressed in approximately 50% of the nasopharyngeal carcinoma samples and was associated with advanced age, high-grade tumors and was an independent predictor of worse disease-free survival. Notably, knockdown of Stathmin 1 suppressed cell cycle progression, proliferation, migration, invasion, xenograft tumor growth, induced apoptosis and potentiated paclitaxel response in nasopharyngeal carcinoma cell lines (CNE1-LMP1 and HNE2 cells) (Wu et al., 2014).
  
Entity Hepatocarcinoma
Note Yuan and colleagues (Yuan et al., 2006) reported a high Stathmin 1 expression in 56% of 156 hepatocarcinoma patients and high Stathmin 1 expression was associated with increased tumor size, tumor grade, metastasis, p53 mutation status and negatively impacted survival in univariate analysis. In agreement, elevated Stathmin 1 levels were also reported by Singer and colleagues (Singer et al., 2007) and were associated with the presence of undifferentiated tumors. Other studies observed an increased Stathmin 1 expression in tumor tissue compared to matched normal tissue, and a positive association between Stathmin 1 overexpression and recurrence or poor prognosis in univariate analysis (Hsieh et al., 2010; Chen et al., 2013b). In hepatocarcinoma cell lines, Stathmin 1 silencing reduced cell proliferation, viability, migration and augmented the response to paclitaxel, vinblastine and cisplatin treatment (Singer et al., 2007; Hsieh et al., 2010; Gan et al., 2010).
  
Entity Endometrial cancer
Note In a multicenter study including 1076 endometrial patients, Stathmin 1 overexpression was detected in 37% of cases and correlated with high grade disease and aneuploidy, and was an independent predictor of metastasis and worse disease specific survival (Trovik et al., 2011). In another study from the same group (Trovik et al., 2010), high Stathmin 1 expression was associated with a higher probability of endometrial cancer recurrence and PI3K activation. Additionally, a study conducted by Salvesen and colleagues (Salvesen et al., 2009), investigating the impact of PI3K activation in endometrial cancer, identified that high Stathmin 1 expression was an independent predictor of aggressive phenotype and worse survival. Of note, Wik and colleagues (Wik et al., 2013) reported that the levels of Stathmin 1 phosphorylation at serine 38 site were associated with poor prognosis, tumor cell proliferation, increased PIK3CA copy number and PI3K activation by multivariate analysis. Werner and colleagues (Werner et al., 2014), using endometrial cancer cell lines, showed that Stathmin 1 silencing potentiated the response to paclitaxel treatment. This finding was confirmed in vivo: endometrial cancer patients with high Stathmin 1 expression had a poor response to paclitaxel therapy (Werner et al., 2014).
  
Entity Bladder cancer and urothelial carcinoma
Note Using quantitative PCR targeting 110 relevant cancer genes, Dubosq and colleagues (Dubosq et al., 2012) detected Stathmin 1 as highly expressed in early recurrence, compared to late or null recurrence cancer in a cohort of 47 bladder cancer patients, suggesting a role for this protein in the time of recurrence. Bhagirath and colleagues (Bhagirath et al., 2012) reported elevated STMN1 mRNA levels in muscle invasive tumors. In agreement, patients with high Stathmin 1 expression under taxane therapy had decreased recurrence-free survival by univariate analysis (Wosnitzer et al., 2011). In a cohort of 58 urothelial carcinoma patients, multivariate analysis revealed that Stathmin 1 positivity was associated with high grade tumors, recurrence and negatively impacted survival (Lin et al., 2009).
  
Entity Colorectal cancer
Note In a cohort of 149 patients with colorectal cancer, high Stathmin 1 levels were an independent predictor of worse overall survival (Zheng et al., 2010). In addition, Stathmin 1 expression was associated with tumor differentiation, invasion and stage of the disease (Zheng et al., 2010). In contrast, Ogino and colleagues (Ogino et al., 2009) showed that, by multivariate analysis, Stathmin 1 positivity had a protective effect on survival in a cohort of 546 colorectal patients (stratified in obese and non-obese individuals). Interestingly, obesity had a negative impact on survival in Stathmin 1 positive patients, but not in Stathmin 1-negative patients (Ogino et al., 2009). A recent study conduced by Tan and colleagues (Tan et al., 2012) corroborated the findings from Zheng and colleagues (Zheng et al., 2010), indicating that high Stathmin 1 levels negatively impacted survival in a cohort of 324 colorectal cancer patients in univariate analysis. Tan and colleagues (Tan et al., 2012) also demonstrated functional evidences that Stathmin 1 is a positive regulator of cell proliferation, clonogenicity, migration and invasion in colorectal cancer cell lines.
  
Entity Gastric cancer
Note Jeon and colleagues (Jeon et al., 2010) reported that a high expression of Stathmin 1 was an independent predictor of shorter recurrence-free survival, and associated with lymph node metastasis and high grade stages in a cohort of 226 gastric cancer patients. The authors, using two different gastric cancer cell lines (SNU638 and SNU16 cells), demonstrated that Stathmin 1 silencing decreased cell proliferation, migration, invasion and xenograft tumor growth (Jeon et al., 2010). Kang and colleagues (Kang et al., 2012), and Ke and colleagues (Ke et al., 2013), identified high Stathmin 1 expression in cell lines and primary cells from gastric cancer and predicted poor prognosis by univariate analysis. Interestingly, Kang and colleagues (Kang et al., 2012) also reported that Stathmin 1 silencing reduced the malignant phenotype in vitro and in vivo, and suggested that miR-223 is involved in the regulation of Stathmin 1 expression in gastric cancer cell lines (AGS and MKN7 cells). Another study, using lentivirus mediated RNAi delivery, also demonstrated that Stathmin 1 silencing reduced cell proliferation, migration and xenograft tumor growth in MKN-45 gastric cancer cells (Akhtar et al., 2013).
  
Entity Prostate cancer
Note Using high-throughput immunoblotting, elevated Stathmin 1 expression was found in metastatic prostate cancer protein extracts (Varambally et al., 2005). Another study reported that Stathmin 1 expression was higher in advanced prostate tumors (Ghosh et al., 2007). Stathmin 1 silencing resulted in cell cycle arrest, reduced clonogenicity and increased apoptosis in prostate cancer cell line (LNCaP cells) (Mistry et al., 2005). In contrast, Stathmin 1 inhibition augmented the epithelial-to-mesenchymal transition and metastasis potential in another prostate cancer cell line (DU145 cells) (Williams et al., 2012).
  
Entity Pheochromocytomas
Note In a study conducted by Sadow and colleagues (Sadow et al., 2008), among the endocrine tumors, high levels of Stathmin 1 were observed in malignant pheochromocytomas. These results were confirmed by two other groups, who reported an overexpression of Stathmin 1 in malignant/metastatic pheochromocytomas compared to benign tumors or normal tissues (Björklund et al., 2010; Lin et al., 2011).
  
Entity Cervical cancer
Note A higher Stathmin 1 expression was found in primary cells and cell lines from cervical carcinoma compared to normal cervical epithelial cells and also in tumor cells compared to matched adjacent non-carcinoma tissue (Xi et al., 2009). Increased Stathmin 1 expression correlated with a worse clinical stage and metastasis (Xi et al., 2009). Another study found Stathmin 1 overexpression in all cervical and rare expression of Stathmin 1 in benign samples; the authors suggest that the analysis of Stathmin 1 may be useful diagnostically in the identification of cervical cancer (Howitt et al., 2013).
  
Entity Glioma
Note In a cohort of 24 glioma patients, increased Stathmin 1 levels were associated with decreased recurrence-free survival in univariate analysis (Ngo et al., 2007). Similar results were observed in a xenograft glioma nitrosourea-treated model (Ngo et al., 2007). Dong and colleagues (Dong et al., 2012) observed that Stathmin 1 expression was aberrantly expressed in vascular endothelial cells from glioma, especially in high grade cases and the Stathmin 1 silencing reduced cell proliferation and invasion, and induced apoptosis in glioma-derived microvascular endothelial cells.
  
Entity Lung cancer
Note Chen and colleagues (Chen et al., 2003) reported a high expression of Stathmin 1 in a cohort of 93 lung adenocarcinoma patients and this expression was associated with poorly differentiated tumors. Stathmin 1 overexpression was also found in primary non-small cell lung tumors matched with normal tissues (Singer et al., 2009). Rosell and colleagues (Rosell et al., 2003) observed that high Stathmin 1 levels negatively affected the time to progression in non-small-cell lung cancer patients, by univariate analysis. Of note, Stathmin 1 inhibition decreased proliferation, migration and invasion in non-small cell lung cancer cell lines (Calu-1 and Calu-6 cells) (Singer et al., 2009).
  
Entity Medulloblastoma
Note Using a microarray approach, Stathmin 1 was identified as differentially expressed in primary medulloblastoma samples and it was associated with unfavorable overall survival (Neben et al., 2004). Accordingly, Kuo and colleagues (Kuo et al., 2009) reported that Stathmin 1 correlated with tumor dissemination and predicted decreased survival in medulloblastoma patients, by univariate analysis in both studies.
  
Entity Pancreatic cancer
Note Lu and colleagues (Lu et al., 2014) reported that Stathmin 1 was overexpressed in pancreatic cancer samples and that high Stathmin 1 levels were correlated with vascular emboli, tumor size, and negatively impacted overall survival in univariate analysis. In addition, Stathmin 1 silencing in pancreatic cancer cells resulted in reduced cell proliferation, clonogenicity and cell cycle arrest (Lu et al., 2014; Jiang et al., 2009).
  
Entity Thyroid cancer
Note Using cDNA microarray approach, Onda and colleagues (Onda et al., 2004) reported that Stathmin 1 was overexpressed in all anaplastic thyroid cancer cell lines analyzed and this was confirmed by immunohistochemical analyses in primary samples. Another study also observed that Stathmin 1 was highly expressed in anaplastic thyroid carcinomas (Sadow et al., 2008).
  
Entity Cholangiocarcinoma
Note In a cohort of 80 extrahepatic cholangiocarcinoma patients, high levels of Stathmin 1 correlated with invasion and shorter recurrence-free survival by multivariate analysis (Watanabe et al., 2014). The authors also demonstrated that Stathmin 1 silencing resulted in reduced cell proliferation capacity and increased sensitivity to paclitaxel treatment in a cholangiocarcinoma cell line (Watanabe et al., 2014).
  
Entity Melanoma
Note In primary melanoma samples, Stathmin 1 was highly expressed in two independent cohorts, but did not impacts survival (Chen et al., 2013a). Stathmin 1 silencing reduced cell proliferation and migration. Furthermore, Stathmin 1 overexpression potentiated both these cell processes in melanoma cell lines (Malme-3M and A375 cells) (Chen et al., 2013a).
  
Entity Mesothelioma
Note Overexpression of Stathmin 1 was found in all mesothelioma cell lines tested (LRK1A, H2052, 211H, H290, MS1, H513 and H28 cells) and also in primary tumors compared to its matched normal tissue (Kim et al., 2007).
  
Entity Pediatric brain cancer
Note Using 2-dimensional differential in-gel electrophoresis, immunohistochemistry and quantitative PCR, Stathmin 1 was identified as highly expressed in primary primitive neuroectodermal tumors compared to ependymomas samples (de Bont et al., 2007).
  
Entity Renal cancer
Note In Wilms tumors, Stathmin 1 was highly expressed in high grade compared to low grade tumors (Takahashi et al., 2002).
  
Entity Sarcoma
Note Belletti and colleagues (Belletti et al., 2008) reported that Stathmin 1 was increased in recurrent and metastatic sarcoma samples. In addition, overexpression of the wild type Stathmin 1 or mutated Stathmin 1 (Q18E, gain-of-function mutation) potentiated the malignant phenotype in the sarcoma cell line HT1080 (Belletti et al., 2008).
  
Entity Salivary cancer
Note Using 2-dimensional differential in-gel electrophoresis, increased Stathmin 1 expression was found in adenoid cystic carcinoma (Nakashima et al., 2006).
  

To be noted

Although Stathmin 1 regulates multiple important cellular functions, Schubart and colleagues (Schubart et al., 1996) initially reported that Stmn1 knockout mice had normal growth, development, reproduction and did not show any aberrant phenotype. Later on, it was observed that Stmn1 knockout mice developed an axonopathy of the central and peripheral nervous systems with aging (Liedtke et al., 2002). In addition, Shumyatsky and colleagues (Shumyatsky et al., 2005) reported that Stmn1 knockout mice had reduced memory in amygdala-dependent fear conditioning, failed to recognize danger environments (Shumyatsky et al., 2005) and exhibited accelerated fear extinction (Martel et al., 2012). Using well-defined mouse models of carcinogenesis and Stmn1 knockout mice, D'Andrea and colleagues (D'Andrea et al., 2012) demonstrated that Stmn1 did not impact on cancer onset. Regarding hematopoietic-related processes, Stmn1 knockout mice presented two human hematopoietic disease phenotypes: megaloblastic anemia and thrombocytosis (Ramlogan-Steel et al., 2012). Notably, Stmn1 knockout mice did not have any that were alterations incompatible with life, and Stathmin 1 inhibition in several types of cancer cells reduced the malignant phenotype, making it an attractive target for anticancer therapies.

External links

Nomenclature
HGNC (Hugo)STMN1   6510
Cards
AtlasSTNM1ID42443ch1p36
Entrez_Gene (NCBI)STMN1  3925  stathmin 1
GeneCards (Weizmann)STMN1
Ensembl hg19 (Hinxton)ENSG00000117632 [Gene_View]  chr1:26210677-26232993 [Contig_View]  STMN1 [Vega]
Ensembl hg38 (Hinxton)ENSG00000117632 [Gene_View]  chr1:26210677-26232993 [Contig_View]  STMN1 [Vega]
ICGC DataPortalENSG00000117632
cBioPortalSTMN1
AceView (NCBI)STMN1
Genatlas (Paris)STMN1
WikiGenes3925
SOURCE (Princeton)STMN1
Genomic and cartography
GoldenPath hg19 (UCSC)STMN1  -     chr1:26210677-26232993 -  1p36.11   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)STMN1  -     1p36.11   [Description]    (hg38-Dec_2013)
EnsemblSTMN1 - 1p36.11 [CytoView hg19]  STMN1 - 1p36.11 [CytoView hg38]
Mapping of homologs : NCBISTMN1 [Mapview hg19]  STMN1 [Mapview hg38]
OMIM151442   
Gene and transcription
Genbank (Entrez)AB209282 AB451319 AB451448 AK054594 AK056768
RefSeq transcript (Entrez)NM_001145454 NM_005563 NM_152497 NM_203399 NM_203401
RefSeq genomic (Entrez)AC_000133 NC_000001 NC_018912 NT_032977 NW_001838576 NW_004929289
Consensus coding sequences : CCDS (NCBI)STMN1
Cluster EST : UnigeneHs.209983 [ NCBI ]
CGAP (NCI)Hs.209983
Alternative Splicing : Fast-db (Paris)GSHG0001879
Alternative Splicing GalleryENSG00000117632
Gene ExpressionSTMN1 [ NCBI-GEO ]     STMN1 [ SEEK ]   STMN1 [ MEM ]
SOURCE (Princeton)Expression in : [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP16949 (Uniprot)
NextProtP16949  [Medical]
With graphics : InterProP16949
Splice isoforms : SwissVarP16949 (Swissvar)
Domaine pattern : Prosite (Expaxy)STATHMIN_1 (PS00563)    STATHMIN_2 (PS01041)    STATHMIN_3 (PS51663)   
Domains : Interpro (EBI)Stathmin_fam   
Related proteins : CluSTrP16949
Domain families : Pfam (Sanger)Stathmin (PF00836)   
Domain families : Pfam (NCBI)pfam00836   
DMDM Disease mutations3925
Blocks (Seattle)P16949
Human Protein AtlasENSG00000117632
Peptide AtlasP16949
HPRD01047
IPIIPI00479997   IPI00921996   IPI00643115   IPI00744618   IPI00065537   IPI00642012   
Protein Interaction databases
DIP (DOE-UCLA)P16949
IntAct (EBI)P16949
FunCoupENSG00000117632
BioGRIDSTMN1
IntegromeDBSTMN1
STRING (EMBL)STMN1
Ontologies - Pathways
QuickGOP16949
Ontology : AmiGOsignal transducer activity  intracellular  cytosol  microtubule  microtubule depolymerization  mitotic spindle organization  signal transduction  axonogenesis  response to virus  tubulin binding  membrane  negative regulation of microtubule polymerization  intracellular signal transduction  positive regulation of cellular component movement  extracellular vesicular exosome  
Ontology : EGO-EBIsignal transducer activity  intracellular  cytosol  microtubule  microtubule depolymerization  mitotic spindle organization  signal transduction  axonogenesis  response to virus  tubulin binding  membrane  negative regulation of microtubule polymerization  intracellular signal transduction  positive regulation of cellular component movement  extracellular vesicular exosome  
Pathways : BIOCARTAStathmin and breast cancer resistance to antimicrotubule agents [Genes]   
Pathways : KEGGMAPK signaling pathway    MicroRNAs in cancer   
Protein Interaction DatabaseSTMN1
DoCM (Curated mutations)STMN1
Wikipedia pathwaysSTMN1
Gene fusion - rearrangements
Polymorphisms : SNP, variants
NCBI Variation ViewerSTMN1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)STMN1
dbVarSTMN1
ClinVarSTMN1
1000_GenomesSTMN1 
Exome Variant ServerSTMN1
SNP (GeneSNP Utah)STMN1
SNP : HGBaseSTMN1
Genetic variants : HAPMAPSTMN1
Genomic VariantsSTMN1  STMN1 [DGVbeta]
Mutations
ICGC Data PortalENSG00000117632 
Somatic Mutations in Cancer : COSMICSTMN1 
CONAN: Copy Number AnalysisSTMN1 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
Diseases
DECIPHER (Syndromes)1:26210677-26232993
Mutations and Diseases : HGMDSTMN1
OMIM151442   
MedgenSTMN1
NextProtP16949 [Medical]
GENETestsSTMN1
Disease Genetic AssociationSTMN1
Huge Navigator STMN1 [HugePedia]  STMN1 [HugeCancerGEM]
snp3D : Map Gene to Disease3925
DGIdb (Drug Gene Interaction db)STMN1
General knowledge
Homologs : HomoloGeneSTMN1
Homology/Alignments : Family Browser (UCSC)STMN1
Phylogenetic Trees/Animal Genes : TreeFamSTMN1
Chemical/Protein Interactions : CTD3925
Chemical/Pharm GKB GenePA35491
Clinical trialSTMN1
Cancer Resource (Charite)ENSG00000117632
Other databases
Probes
Litterature
PubMed160 Pubmed reference(s) in Entrez
CoreMineSTMN1
GoPubMedSTMN1
iHOPSTMN1

Bibliography

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Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis.
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EMBO J. 1997 Sep 15;16(18):5537-49.
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Role for protein phosphatases in the cell-cycle-regulated phosphorylation of stathmin.
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Biochem J. 1998 Aug 15;334 ( Pt 1):23-9.
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Stathmin and its phosphoprotein family: general properties, biochemical and functional interaction with tubulin.
Curmi PA, Gavet O, Charbaut E, Ozon S, Lachkar-Colmerauer S, Manceau V, Siavoshian S, Maucuer A, Sobel A.
Cell Struct Funct. 1999 Oct;24(5):345-57.
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Correlation of oncoprotein 18/stathmin expression in human breast cancer with established prognostic factors.
Brattsand G.
Br J Cancer. 2000 Aug;83(3):311-8.
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Overexpression of stathmin in breast carcinomas points out to highly proliferative tumours.
Curmi PA, Nogues C, Lachkar S, Carelle N, Gonthier MP, Sobel A, Lidereau R, Bieche I.
Br J Cancer. 2000 Jan;82(1):142-50.
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The phosphoprotein Op18/stathmin is differentially expressed in ovarian cancer.
Price DK, Ball JR, Bahrani-Mostafavi Z, Vachris JC, Kaufman JS, Naumann RW, Higgins RV, Hall JB.
Cancer Invest. 2000;18(8):722-30.
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Effects of stathmin inhibition on the mitotic spindle.
Iancu C, Mistry SJ, Arkin S, Wallenstein S, Atweh GF.
J Cell Sci. 2001 Mar;114(Pt 5):909-16.
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Stathmin-deficient mice develop an age-dependent axonopathy of the central and peripheral nervous systems.
Liedtke W, Leman EE, Fyffe RE, Raine CS, Schubart UK.
Am J Pathol. 2002 Feb;160(2):469-80.
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Transforming properties of a Q18-->E mutation of the microtubule regulator Op18.
Misek DE, Chang CL, Kuick R, Hinderer R, Giordano TJ, Beer DG, Hanash SM.
Cancer Cell. 2002 Sep;2(3):217-28.
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Gene expression profiling of favorable histology Wilms tumors and its correlation with clinical features.
Takahashi M, Yang XJ, Lavery TT, Furge KA, Williams BO, Tretiakova M, Montag A, Vogelzang NJ, Re GG, Garvin AJ, Soderhall S, Kagawa S, Hazel-Martin D, Nordenskjold A, Teh BT.
Cancer Res. 2002 Nov 15;62(22):6598-605.
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Overexpression of oncoprotein 18 correlates with poor differentiation in lung adenocarcinomas.
Chen G, Wang H, Gharib TG, Huang CC, Thomas DG, Shedden KA, Kuick R, Taylor JM, Kardia SL, Misek DE, Giordano TJ, Iannettoni MD, Orringer MB, Hanash SM, Beer DG.
Mol Cell Proteomics. 2003 Feb;2(2):107-16. Epub 2003 Feb 12.
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Transcripts in pretreatment biopsies from a three-arm randomized trial in metastatic non-small-cell lung cancer.
Rosell R, Scagliotti G, Danenberg KD, Lord RV, Bepler G, Novello S, Cooc J, Crino L, Sanchez JJ, Taron M, Boni C, De Marinis F, Tonato M, Marangolo M, Gozzelino F, Di Costanzo F, Rinaldi M, Salonga D, Stephens C.
Oncogene. 2003 Jun 5;22(23):3548-53.
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Microarray-based screening for molecular markers in medulloblastoma revealed STK15 as independent predictor for survival.
Neben K, Korshunov A, Benner A, Wrobel G, Hahn M, Kokocinski F, Golanov A, Joos S, Lichter P.
Cancer Res. 2004 May 1;64(9):3103-11.
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Comprehensive gene expression profiling of anaplastic thyroid cancers with cDNA microarray of 25 344 genes.
Onda M, Emi M, Yoshida A, Miyamoto S, Akaishi J, Asaka S, Mizutani K, Shimizu K, Nagahama M, Ito K, Tanaka T, Tsunoda T.
Endocr Relat Cancer. 2004 Dec;11(4):843-54.
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Identification of differentially expressed proteins in oral squamous cell carcinoma using a global proteomic approach.
Koike H, Uzawa K, Nakashima D, Shimada K, Kato Y, Higo M, Kouzu Y, Endo Y, Kasamatsu A, Tanzawa H.
Int J Oncol. 2005 Jul;27(1):59-67.
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Targeting stathmin in prostate cancer.
Mistry SJ, Bank A, Atweh GF.
Mol Cancer Ther. 2005 Dec;4(12):1821-9.
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stathmin, a gene enriched in the amygdala, controls both learned and innate fear.
Shumyatsky GP, Malleret G, Shin RM, Takizawa S, Tully K, Tsvetkov E, Zakharenko SS, Joseph J, Vronskaya S, Yin D, Schubart UK, Kandel ER, Bolshakov VY.
Cell. 2005 Nov 18;123(4):697-709.
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Integrative genomic and proteomic analysis of prostate cancer reveals signatures of metastatic progression.
Varambally S, Yu J, Laxman B, Rhodes DR, Mehra R, Tomlins SA, Shah RB, Chandran U, Monzon FA, Becich MJ, Wei JT, Pienta KJ, Ghosh D, Rubin MA, Chinnaiyan AM.
Cancer Cell. 2005 Nov;8(5):393-406.
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Aneugenic activity of Op18/stathmin is potentiated by the somatic Q18-->e mutation in leukemic cells.
Holmfeldt P, Brannstrom K, Stenmark S, Gullberg M.
Mol Biol Cell. 2006 Jul;17(7):2921-30. Epub 2006 Apr 19.
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Overexpression of stathmin in oral squamous-cell carcinoma: correlation with tumour progression and poor prognosis.
Kouzu Y, Uzawa K, Koike H, Saito K, Nakashima D, Higo M, Endo Y, Kasamatsu A, Shiiba M, Bukawa H, Yokoe H, Tanzawa H.
Br J Cancer. 2006 Mar 13;94(5):717-23.
PMID 16495930
 
Protein expression profiling identifies maspin and stathmin as potential biomarkers of adenoid cystic carcinoma of the salivary glands.
Nakashima D, Uzawa K, Kasamatsu A, Koike H, Endo Y, Saito K, Hashitani S, Numata T, Urade M, Tanzawa H.
Int J Cancer. 2006 Feb 1;118(3):704-13.
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Stathmin overexpression cooperates with p53 mutation and osteopontin overexpression, and is associated with tumour progression, early recurrence, and poor prognosis in hepatocellular carcinoma.
Yuan RH, Jeng YM, Chen HL, Lai PL, Pan HW, Hsieh FJ, Lin CY, Lee PH, Hsu HC.
J Pathol. 2006 Aug;209(4):549-58.
PMID 16739096
 
Identification of novel biomarkers in pediatric primitive neuroectodermal tumors and ependymomas by proteome-wide analysis.
de Bont JM, den Boer ML, Kros JM, Passier MM, Reddingius RE, Smitt PA, Luider TM, Pieters R.
J Neuropathol Exp Neurol. 2007 Jun;66(6):505-16.
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Increased expression and differential phosphorylation of stathmin may promote prostate cancer progression.
Ghosh R, Gu G, Tillman E, Yuan J, Wang Y, Fazli L, Rennie PS, Kasper S.
Prostate. 2007 Jul 1;67(10):1038-52.
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Stathmin is overexpressed in malignant mesothelioma.
Kim JY, Harvard C, You L, Xu Z, Kuchenbecker K, Baehner R, Jablons D.
Anticancer Res. 2007 Jan-Feb;27(1A):39-44.
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The 1p-encoded protein stathmin and resistance of malignant gliomas to nitrosoureas.
Ngo TT, Peng T, Liang XJ, Akeju O, Pastorino S, Zhang W, Kotliarov Y, Zenklusen JC, Fine HA, Maric D, Wen PY, De Girolami U, Black PM, Wu WW, Shen RF, Jeffries NO, Kang DW, Park JK.
J Natl Cancer Inst. 2007 Apr 18;99(8):639-52.
PMID 17440165
 
Functional pathway characterized by gene expression analysis of supraclavicular lymph node metastasis-positive breast cancer.
Oishi Y, Nagasaki K, Miyata S, Matsuura M, Nishimura S, Akiyama F, Iwai T, Miki Y.
J Hum Genet. 2007;52(3):271-9. Epub 2007 Feb 7.
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Poor prognosis in carcinoma is associated with a gene expression signature of aberrant PTEN tumor suppressor pathway activity.
Saal LH, Johansson P, Holm K, Gruvberger-Saal SK, She QB, Maurer M, Koujak S, Ferrando AA, Malmstrom P, Memeo L, Isola J, Bendahl PO, Rosen N, Hibshoosh H, Ringner M, Borg A, Parsons R.
Proc Natl Acad Sci U S A. 2007 May 1;104(18):7564-9. Epub 2007 Apr 23.
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Proteomic signatures in laryngeal squamous cell carcinoma.
Sewell DA, Yuan CX, Robertson E.
ORL J Otorhinolaryngol Relat Spec. 2007;69(2):77-84. Epub 2006 Nov 24.
PMID 17127822
 
Protumorigenic overexpression of stathmin/Op18 by gain-of-function mutation in p53 in human hepatocarcinogenesis.
Singer S, Ehemann V, Brauckhoff A, Keith M, Vreden S, Schirmacher P, Breuhahn K.
Hepatology. 2007 Sep;46(3):759-68.
PMID 17663418
 
Stathmin activity influences sarcoma cell shape, motility, and metastatic potential.
Belletti B, Nicoloso MS, Schiappacassi M, Berton S, Lovat F, Wolf K, Canzonieri V, D'Andrea S, Zucchetto A, Friedl P, Colombatti A, Baldassarre G.
Mol Biol Cell. 2008 May;19(5):2003-13. doi: 10.1091/mbc.E07-09-0894. Epub 2008 Feb 27.
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Identification of novel nasopharyngeal carcinoma biomarkers by laser capture microdissection and proteomic analysis.
Cheng AL, Huang WG, Chen ZC, Peng F, Zhang PF, Li MY, Li F, Li JL, Li C, Yi H, Yi B, Xiao ZQ.
Clin Cancer Res. 2008 Jan 15;14(2):435-45. doi: 10.1158/1078-0432.CCR-07-1215.
PMID 18223218
 
Prediction of survival in multiple myeloma based on gene expression profiles reveals cell cycle and chromosomal instability signatures in high-risk patients and hyperdiploid signatures in low-risk patients: a study of the Intergroupe Francophone du Myelome.
Decaux O, Lode L, Magrangeas F, Charbonnel C, Gouraud W, Jezequel P, Attal M, Harousseau JL, Moreau P, Bataille R, Campion L, Avet-Loiseau H, Minvielle S; Intergroupe Francophone du Myelome.
J Clin Oncol. 2008 Oct 10;26(29):4798-805. doi: 10.1200/JCO.2007.13.8545. Epub 2008 Jun 30.
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The prognostic value of Stathmin-1, S100A2, and SYK proteins in ER-positive primary breast cancer patients treated with adjuvant tamoxifen monotherapy: an immunohistochemical study.
Golouh R, Cufer T, Sadikov A, Nussdorfer P, Usher PA, Brunner N, Schmitt M, Lesche R, Maier S, Timmermans M, Foekens JA, Martens JW.
Breast Cancer Res Treat. 2008 Jul;110(2):317-26. Epub 2007 Sep 13.
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Proteins induced by telomere dysfunction and DNA damage represent biomarkers of human aging and disease.
Jiang H, Schiffer E, Song Z, Wang J, Zurbig P, Thedieck K, Moes S, Bantel H, Saal N, Jantos J, Brecht M, Jeno P, Hall MN, Hager K, Manns MP, Hecker H, Ganser A, Dohner K, Bartke A, Meissner C, Mischak H, Ju Z, Rudolph KL.
Proc Natl Acad Sci U S A. 2008 Aug 12;105(32):11299-304. doi: 10.1073/pnas.0801457105. Epub 2008 Aug 11.
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Stathmin 1: a novel therapeutic target for anticancer activity.
Rana S, Maples PB, Senzer N, Nemunaitis J.
Expert Rev Anticancer Ther. 2008 Sep;8(9):1461-70. doi: 10.1586/14737140.8.9.1461. (REVIEW)
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Stathmin expression in pheochromocytomas, paragangliomas, and in other endocrine tumors.
Sadow PM, Rumilla KM, Erickson LA, Lloyd RV.
Endocr Pathol. 2008 Summer;19(2):97-103. doi: 10.1007/s12022-008-9028-0.
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Prognostic significance of stathmin expression in correlation with metastasis and clinicopathological characteristics in human ovarian carcinoma.
Wei SH, Lin F, Wang X, Gao P, Zhang HZ.
Acta Histochem. 2008;110(1):59-65. Epub 2007 Dec 3.
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Overexpression of class III beta-tubulin predicts good response to taxane-based chemotherapy in ovarian clear cell adenocarcinoma.
Aoki D, Oda Y, Hattori S, Taguchi K, Ohishi Y, Basaki Y, Oie S, Suzuki N, Kono S, Tsuneyoshi M, Ono M, Yanagawa T, Kuwano M.
Clin Cancer Res. 2009 Feb 15;15(4):1473-80. doi: 10.1158/1078-0432.CCR-08-1274.
PMID 19228748
 
Down-regulation of stathmin is required for TGF-beta inducible early gene 1 induced growth inhibition of pancreatic cancer cells.
Jiang L, Chen Y, Chan CY, Wang X, Lin L, He ML, Lin MC, Yew DT, Sung JJ, Li JC, Kung HF.
Cancer Lett. 2009 Feb 8;274(1):101-8. doi: 10.1016/j.canlet.2008.09.017. Epub 2008 Oct 18.
PMID 18930345
 
High expression of stathmin protein predicts a fulminant course in medulloblastoma.
Kuo MF, Wang HS, Kuo QT, Shun CT, Hsu HC, Yang SH, Yuan RH.
J Neurosurg Pediatr. 2009 Jul;4(1):74-80. doi: 10.3171/2009.2.PEDS08287.
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Expression of stathmin in localized upper urinary tract urothelial carcinoma: correlations with prognosis.
Lin WC, Chen SC, Hu FC, Chueh SC, Pu YS, Yu HJ, Huang KH.
Urology. 2009 Dec;74(6):1264-9. doi: 10.1016/j.urology.2009.04.088. Epub 2009 Oct 2.
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A cohort study of STMN1 expression in colorectal cancer: body mass index and prognosis.
Ogino S, Nosho K, Baba Y, Kure S, Shima K, Irahara N, Toyoda S, Chen L, Kirkner GJ, Wolpin BM, Chan AT, Giovannucci EL, Fuchs CS.
Am J Gastroenterol. 2009 Aug;104(8):2047-56. doi: 10.1038/ajg.2009.281. Epub 2009 Jun 9.
PMID 19513025
 
Integrated genomic profiling of endometrial carcinoma associates aggressive tumors with indicators of PI3 kinase activation.
Salvesen HB, Carter SL, Mannelqvist M, Dutt A, Getz G, Stefansson IM, Raeder MB, Sos ML, Engelsen IB, Trovik J, Wik E, Greulich H, Bo TH, Jonassen I, Thomas RK, Zander T, Garraway LA, Oyan AM, Sellers WR, Kalland KH, Meyerson M, Akslen LA, Beroukhim R.
Proc Natl Acad Sci U S A. 2009 Mar 24;106(12):4834-9. doi: 10.1073/pnas.0806514106. Epub 2009 Mar 4.
PMID 19261849
 
Coordinated expression of stathmin family members by far upstream sequence element-binding protein-1 increases motility in non-small cell lung cancer.
Singer S, Malz M, Herpel E, Warth A, Bissinger M, Keith M, Muley T, Meister M, Hoffmann H, Penzel R, Gdynia G, Ehemann V, Schnabel PA, Kuner R, Huber P, Schirmacher P, Breuhahn K.
Cancer Res. 2009 Mar 15;69(6):2234-43. doi: 10.1158/0008-5472.CAN-08-3338. Epub 2009 Mar 3.
PMID 19258502
 
Stathmin and tubulin expression and survival of ovarian cancer patients receiving platinum treatment with and without paclitaxel.
Su D, Smith SM, Preti M, Schwartz P, Rutherford TJ, Menato G, Danese S, Ma S, Yu H, Katsaros D.
Cancer. 2009 Jun 1;115(11):2453-63. doi: 10.1002/cncr.24282.
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Expression of stathmin/op18 as a significant prognostic factor for cervical carcinoma patients.
Xi W, Rui W, Fang L, Ke D, Ping G, Hui-Zhong Z.
J Cancer Res Clin Oncol. 2009 Jun;135(6):837-46. doi: 10.1007/s00432-008-0520-1. Epub 2008 Nov 26.
PMID 19034510
 
Stathmin as a marker for malignancy in pheochromocytomas.
Bjorklund P, Cupisti K, Fryknas M, Isaksson A, Willenberg HS, Akerstrom G, Hellman P, Westin G.
Exp Clin Endocrinol Diabetes. 2010 Jan;118(1):27-30. doi: 10.1055/s-0029-1202789. Epub 2009 May 15.
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Up-regulated expression of stathmin may be associated with hepatocarcinogenesis.
Gan L, Guo K, Li Y, Kang X, Sun L, Shu H, Liu Y.
Oncol Rep. 2010 Apr;23(4):1037-43.
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Stathmin1 overexpression associated with polyploidy, tumor-cell invasion, early recurrence, and poor prognosis in human hepatoma.
Hsieh SY, Huang SF, Yu MC, Yeh TS, Chen TC, Lin YJ, Chang CJ, Sung CM, Lee YL, Hsu CY.
Mol Carcinog. 2010 May;49(5):476-87. doi: 10.1002/mc.20627.
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Overexpression of stathmin1 in the diffuse type of gastric cancer and its roles in proliferation and migration of gastric cancer cells.
Jeon TY, Han ME, Lee YW, Lee YS, Kim GH, Song GA, Hur GY, Kim JY, Kim HJ, Yoon S, Baek SY, Kim BS, Kim JB, Oh SO.
Br J Cancer. 2010 Feb 16;102(4):710-8. doi: 10.1038/sj.bjc.6605537. Epub 2010 Jan 19.
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Stathmin is superior to AKT and phospho-AKT staining for the detection of phosphoinositide 3-kinase activation and aggressive endometrial cancer.
Trovik J, Wik E, Stefansson I, Carter SL, Beroukhim R, Oyan AM, Kalland KH, Akslen LA, Salvesen HB.
Histopathology. 2010 Oct;57(4):641-6. doi: 10.1111/j.1365-2559.2010.03661.x.
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Stathmin, a new target of PRL-3 identified by proteomic methods, plays a key role in progression and metastasis of colorectal cancer.
Zheng P, Liu YX, Chen L, Liu XH, Xiao ZQ, Zhao L, Li GQ, Zhou J, Ding YQ, Li JM.
J Proteome Res. 2010 Oct 1;9(10):4897-905. doi: 10.1021/pr100712t.
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Stathmin: a protein with many tasks. New biomarker and potential target in cancer.
Belletti B, Baldassarre G.
Expert Opin Ther Targets. 2011 Nov;15(11):1249-66. doi: 10.1517/14728222.2011.620951. Epub 2011 Oct 7.
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Stathmin 1, a marker of PI3K pathway activation and regulator of microtubule dynamics, is expressed in early pelvic serous carcinomas.
Karst AM, Levanon K, Duraisamy S, Liu JF, Hirsch MS, Hecht JL, Drapkin R.
Gynecol Oncol. 2011 Oct;123(1):5-12. doi: 10.1016/j.ygyno.2011.05.021. Epub 2011 Jun 17.
PMID 21683992
 
Siva1 suppresses epithelial-mesenchymal transition and metastasis of tumor cells by inhibiting stathmin and stabilizing microtubules.
Li N, Jiang P, Du W, Wu Z, Li C, Qiao M, Yang X, Wu M.
Proc Natl Acad Sci U S A. 2011 Aug 2;108(31):12851-6. doi: 10.1073/pnas.1017372108. Epub 2011 Jul 18.
PMID 21768358
 
Stathmin immunoreactivity in phaeochromocytomas and paragangliomas: differential expression between benign and malignant neoplasms.
Lin WC, Chen SC, Chuang YT, Kuo KL, Huang KH.
Asian J Surg. 2011 Jan;34(1):15-22. doi: 10.1016/S1015-9584(11)60013-4.
PMID 21515208
 
Stathmin overexpression identifies high-risk patients and lymph node metastasis in endometrial cancer.
Trovik J, Wik E, Stefansson IM, Marcickiewicz J, Tingulstad S, Staff AC, Njolstad TS; MoMaTec Study Group, Vandenput I, Amant F, Akslen LA, Salvesen HB.
Clin Cancer Res. 2011 May 15;17(10):3368-77. doi: 10.1158/1078-0432.CCR-10-2412. Epub 2011 Jan 17.
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Predictive value of microtubule associated proteins tau and stathmin in patients with nonmuscle invasive bladder cancer receiving adjuvant intravesical taxane therapy.
Wosnitzer MS, Domingo-Domenech J, Castillo-Martin M, Ritch C, Mansukhani M, Petrylack DP, Benson MC, McKiernan JM, Cordon-Cardo C.
J Urol. 2011 Nov;186(5):2094-100. doi: 10.1016/j.juro.2011.06.051. Epub 2011 Sep 23.
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Stathmin expression and its relationship to microtubule-associated protein tau and outcome in breast cancer.
Baquero MT, Hanna JA, Neumeister V, Cheng H, Molinaro AM, Harris LN, Rimm DL.
Cancer. 2012 Oct 1;118(19):4660-9. doi: 10.1002/cncr.27453. Epub 2012 Feb 22.
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Expression of CD147, BIGH3 and Stathmin and their potential role as diagnostic marker in patients with urothelial carcinoma of the bladder.
Bhagirath D, Abrol N, Khan R, Sharma M, Seth A, Sharma A.
Clin Chim Acta. 2012 Oct 9;413(19-20):1641-6. doi: 10.1016/j.cca.2012.05.005. Epub 2012 May 14.
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Alteration of G1/S transition regulators influences recurrences in head and neck squamous carcinomas.
Canzonieri V, Barzan L, Franchin G, Vaccher E, Talamini R, Sulfaro S, Baldassarre G.
J Cell Physiol. 2012 Jan;227(1):233-8. doi: 10.1002/jcp.22723.
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Stathmin is dispensable for tumor onset in mice.
D'Andrea S, Berton S, Segatto I, Fabris L, Canzonieri V, Colombatti A, Vecchione A, Belletti B, Baldassarre G.
PLoS One. 2012;7(9):e45561. doi: 10.1371/journal.pone.0045561. Epub 2012 Sep 20.
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Stathmin expression in glioma-derived microvascular endothelial cells: a novel therapeutic target.
Dong B, Mu L, Qin X, Qiao W, Liu X, Yang L, Xue L, Rainov NG, Liu X.
Oncol Rep. 2012 Mar;27(3):714-8. doi: 10.3892/or.2011.1525. Epub 2011 Oct 31.
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Identification of a three-gene expression signature of early recurrence in non-muscle-invasive urothelial cell carcinoma of the bladder.
Dubosq F, Ploussard G, Soliman H, Turpin E, Latil A, Desgrandchamps F, de The H, Mongiat-Artus P.
Urol Oncol. 2012 Nov-Dec;30(6):833-40. doi: 10.1016/j.urolonc.2011.02.018. Epub 2011 Apr 13.
PMID 21489836
 
Stathmin1 plays oncogenic role and is a target of microRNA-223 in gastric cancer.
Kang W, Tong JH, Chan AW, Lung RW, Chau SL, Wong QW, Wong N, Yu J, Cheng AS, To KF.
PLoS One. 2012;7(3):e33919. doi: 10.1371/journal.pone.0033919. Epub 2012 Mar 28.
PMID 22470493
 
Murine GRPR and stathmin control in opposite directions both cued fear extinction and neural activities of the amygdala and prefrontal cortex.
Martel G, Hevi C, Wong A, Zushida K, Uchida S, Shumyatsky GP.
PLoS One. 2012;7(2):e30942. doi: 10.1371/journal.pone.0030942. Epub 2012 Feb 1.
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The Role of Stathmin, a Regulator of Mitosis, in Hematopoiesis.
Ramlogan-Steel CA, Steel JC, Fathallah H, Iancu-Rubin C, Soleimani M, Dong, Atweh GF.
Blood (ASH Annual Meeting Abstracts). 2012 120(21): Abstract #3453.
 
Proteomic analysis of colorectal cancer metastasis: stathmin-1 revealed as a player in cancer cell migration and prognostic marker.
Tan HT, Wu W, Ng YZ, Zhang X, Yan B, Ong CW, Tan S, Salto-Tellez M, Hooi SC, Chung MC.
J Proteome Res. 2012 Feb 3;11(2):1433-45. doi: 10.1021/pr2010956. Epub 2012 Jan 10.
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Inhibition of stathmin1 accelerates the metastatic process.
Williams K, Ghosh R, Giridhar PV, Gu G, Case T, Belcher SM, Kasper S.
Cancer Res. 2012 Oct 15;72(20):5407-17. doi: 10.1158/0008-5472.CAN-12-1158. Epub 2012 Aug 21.
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Lentiviral-mediated RNA interference targeting stathmin1 gene in human gastric cancer cells inhibits proliferation in vitro and tumor growth in vivo.
Akhtar J, Wang Z, Zhang ZP, Bi MM.
J Transl Med. 2013 Sep 16;11:212. doi: 10.1186/1479-5876-11-212.
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Stathmin 1 is a potential novel oncogene in melanoma.
Chen J, Abi-Daoud M, Wang A, Yang X, Zhang X, Feilotter HE, Tron VA.
Oncogene. 2013a Mar 7;32(10):1330-7. doi: 10.1038/onc.2012.141. Epub 2012 Jun 4.
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The E2F transcription factor 1 transactives stathmin 1 in hepatocellular carcinoma.
Chen YL, Uen YH, Li CF, Horng KC, Chen LR, Wu WR, Tseng HY, Huang HY, Wu LC, Shiue YL.
Ann Surg Oncol. 2013b Nov;20(12):4041-54. doi: 10.1245/s10434-012-2519-8. Epub 2012 Aug 22.
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Stathmin-1 expression as a complement to p16 helps identify high-grade cervical intraepithelial neoplasia with increased specificity.
Howitt BE, Nucci MR, Drapkin R, Crum CP, Hirsch MS.
Am J Surg Pathol. 2013 Jan;37(1):89-97. doi: 10.1097/PAS.0b013e3182753f5a.
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Overexpression of stathmin 1 is associated with poor prognosis of patients with gastric cancer.
Ke B, Wu LL, Liu N, Zhang RP, Wang CL, Liang H.
Tumour Biol. 2013 Oct;34(5):3137-45. doi: 10.1007/s13277-013-0882-0. Epub 2013 Jun 13.
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Another look at follicular lymphoma: immunophenotypic and molecular analyses identify distinct follicular lymphoma subgroups.
Marafioti T, Copie-Bergman C, Calaminici M, Paterson JC, Shende VH, Liu H, Baia M, Ramsay AD, Agostinelli C, Briere J, Clear A, Du MQ, Piccaluga PP, Masir N, Nacheva EP, Sujobert P, Shanmugam K, Grogan TM, Brooks SP, Khwaja A, Ardeshna K, Townsend W, Pileri SA, Haioun C, Linch D, Gribben JG, Gaulard P, Isaacson PG.
Histopathology. 2013 May;62(6):860-75. doi: 10.1111/his.12076. Epub 2013 Mar 20.
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Cell cycle inhibition therapy that targets stathmin in in vitro and in vivo models of breast cancer.
Miceli C, Tejada A, Castaneda A, Mistry SJ.
Cancer Gene Ther. 2013 May;20(5):298-307. doi: 10.1038/cgt.2013.21. Epub 2013 Apr 26.
PMID 23618950
 
Stathmin regulates mutant p53 stability and transcriptional activity in ovarian cancer.
Sonego M, Schiappacassi M, Lovisa S, Dall'Acqua A, Bagnoli M, Lovat F, Libra M, D'Andrea S, Canzonieri V, Militello L, Napoli M, Giorda G, Pivetta B, Mezzanzanica D, Barbareschi M, Valeri B, Canevari S, Colombatti A, Belletti B, Del Sal G, Baldassarre G.
EMBO Mol Med. 2013 May;5(5):707-22. doi: 10.1002/emmm.201201504. Epub 2013 Apr 22.
PMID 23610071
 
High phospho-Stathmin(Serine38) expression identifies aggressive endometrial cancer and suggests an association with PI3K inhibition.
Wik E, Birkeland E, Trovik J, Werner HM, Hoivik EA, Mjos S, Krakstad C, Kusonmano K, Mauland K, Stefansson IM, Holst F, Petersen K, Oyan AM, Simon R, Kalland KH, Ricketts W, Akslen LA, Salvesen HB.
Clin Cancer Res. 2013 May 1;19(9):2331-41. doi: 10.1158/1078-0432.CCR-12-3413. Epub 2013 Mar 28.
PMID 23538402
 
Overexpression of stathmin 1 confers an independent prognostic indicator in nasopharyngeal carcinoma.
Hsu HP, Li CF, Lee SW, Wu WR, Chen TJ, Chang KY, Liang SS, Tsai CJ, Shiue YL.
Tumour Biol. 2014 Mar;35(3):2619-29. doi: 10.1007/s13277-013-1345-3. Epub 2013 Nov 12.
PMID 24218338
 
Stathmin, interacting with Nf-kB, promotes tumor growth and predicts poor prognosis of pancreatic cancer.
Lu Y, Liu C, Cheng H, Xu Y, Jiang J, Xu J, Long J, Liu L, Yu X.
Curr Mol Med. 2014 Mar;14(3):328-39.
PMID 24588766
 
Stathmin 1 is involved in the highly proliferative phenotype of high-risk myelodysplastic syndromes and acute leukemia cells.
Machado-Neto JA, de Melo Campos P, Favaro P, Lazarini M, Lorand-Metze I, Costa FF, Olalla Saad ST, Traina F.
Leuk Res. 2014a Feb;38(2):251-7. doi: 10.1016/j.leukres.2013.11.013. Epub 2013 Dec 1.
PMID 24355524
 
Stathmin 1 in normal and malignant hematopoiesis.
Machado-Neto JA, Saad ST, Traina F.
BMB Rep. 2014b Mar 18. pii: 2687. [Epub ahead of print]
PMID 24667172
 
Stathmin1 regulates p27 expression, proliferation and drug resistance, resulting in poor clinical prognosis in cholangiocarcinoma.
Watanabe A, Suzuki H, Yokobori T, Tsukagoshi M, Altan B, Kubo N, Suzuki S, Araki K, Wada S, Kashiwabara K, Hosouchi Y, Kuwano H.
Cancer Sci. 2014 Jun;105(6):690-6. doi: 10.1111/cas.12417. Epub 2014 May 27.
PMID 24708177
 
Stathmin protein level, a potential predictive marker for taxane treatment response in endometrial cancer.
Werner HM, Trovik J, Halle MK, Wik E, Akslen LA, Birkeland E, Bredholt T, Tangen IL, Krakstad C, Salvesen HB.
PLoS One. 2014 Feb 25;9(2):e90141. doi: 10.1371/journal.pone.0090141. eCollection 2014.
PMID 24587245
 
A combination of paclitaxel and siRNA-mediated silencing of Stathmin inhibits growth and promotes apoptosis of nasopharyngeal carcinoma cells.
Wu Y, Tang M, Wu Y, Weng X, Yang L, Xu W, Yi W, Gao J, Bode AM, Dong Z, Cao Y.
Cell Oncol (Dordr). 2014 Feb;37(1):53-67. doi: 10.1007/s13402-013-0163-3. Epub 2013 Dec 5.
PMID 24306928
 
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Written05-2014João Agostinho Machado-Neto, Fabiola Traina
Hematology and Hemotherapy Center-University of Campinas/Hemocentro-Unicamp, Instituto Nacional de Ciencia e Tecnologia do Sangue, Campinas, Sao Paulo, Brazil (JAMN, FT); Department of Internal Medicine, University of Sao Paulo at Ribeirao Preto Medical School, Ribeirao Preto, Sao Paulo, Brazil (FT)

Citation

This paper should be referenced as such :
Machado-Neto JA, Traina F
STMN1 (stathmin 1);
Atlas Genet Cytogenet Oncol Haematol. May 2014
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/STMN1ID42443ch1p36.html

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