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Taking over the Atlas
Dear Colleagues,
The Atlas, once more, is in great danger, and I will have to proceed to a collective economic lay-off of all the team involved in the Atlas before the begining of April 2015 (a foundation having suddenly withdrawn its commitment to support the Atlas). I ask you herein if any Scientific Society (a Society of Cytogenetics, of Clinical Genetics, of Hematology, or a Cancer Society, or any other...), any University and/or Hospital, any Charity, or any database would be interested in taking over the Atlas, in whole or in part. If taking charge of the whole lot is too big, a consortium of various actors could be the solution (I am myself trying to find partners). Could you please spread the information, contact the relevant authorities, and find partners.
Survival of the Atlas will be critically dependant upon your ability to find solutions (and urgently!).
Kind regards.
Jean-Loup Huret
Donations are also welcome
If each casual visitor gives 3 Euros or Dollars, the Atlas is saved in a week !
If each professional gives 100 Euros or Dollars once a year (now), the Atlas is saved in 2 weeks !
Don't let the Atlas imminent demise
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XPO1 (exportin 1 (CRM1 homolog, yeast))


Other namesCRM1
HGNC (Hugo) XPO1
LocusID (NCBI) 7514
Location 2p15
Location_base_pair Starts at 61705069 and ends at 61765418 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Note The human XPO1/hCRM1 gene is localized on the 2p16 region (Fornerod et al., 1997a).


Transcription The human XPO1/hCRM1 gene is transcribed in a cell cycle-dependent manner, with the onset of mRNA transcription taking place in late G1 phase and peaking in the G2/M phases of the cell cycle (Kudo et al., 1997). NFY/CBP, Sp1 and p53 transcription factors are reported to interact with the XPO1/hCRM1 gene promoter and play an important role in XPO1/hCRM1 promoter activity in transformed and cancer cells (van der Watt and Leaner, 2011).


Note A human protein, originally named CC112 based on its apparent molecular weight, was identified in a search for interacting partners of CAN/NUP214, a nucleoporin regarded as a proto-oncogenic factor. CAN was implicated in acute myeloid leukemia and in myelodysplastic syndrome (von Lindern et al., 1992) as part of the DEK-CAN fusion gene generated in the translocation t(6;9)(p23;q34). Another potentially oncogenic fusion protein involving CAN was identified in a patient with acute undifferentiated leukemia, in which case the t(6;9) yielded a SET-CAN fusion. Wild-type CAN is identical to the nucleoporin NUP214. CC112 was capable of interacting with both wild-type CAN/NUP214 and with both its fusion proteins, DEK-CAN and SET-CAN, suggesting potential roles in proliferation of cancer cells (Fornerod et al., 1996).
Description The human XPO1/CRM1 protein is composed of 1071 aminoacidic residues with a molecular weight of 112 kDa (Fornerod et al., 1997b). It is a modular protein composed of several fuctional domains:
- The N-terminal region shares sequence similarity with importin β in a region called the CRIME domain (acronym for CRM1, importin beta etc.). This domain interacts with the GTPase RAN. In the GTP-bound form, RAN stabilizes export complex formed by CRM1 and NES-containing proteins.
- Most of the XPO1/CRM1 protein is composed of 19 HEAT repeat motifs. HEAT repeat 8 contains an acidic loop which cooperates with the CRIME domain in RANGTP binding.
- The central region of XPO1/CRM1 is involved in NES binding. Cys528, lying in this region, is specifically blocked by the inhibitor leptomycin B (LMB), which therefore blocks the export activity of XPO1/CRM1 (Wolff et al., 1997).
- The C-terminal region is thought to modulate the affinity of XPO1/CRM1 for its cargoes.

The structure of the region corresponding to residues 707-1034 (C-terminal region) was elucidated by X-ray crystallography (Petosa et al., 2004).
The structure of XPO1/CRM1 complexed to various NESs and to RANGTP has been solved (Güttler et al., 2010).

Expression XPO1/CRM1 protein levels remain constant throughout the cell cycle (Kudo et al., 1997).
Localisation Due to its function as a shuttling nuclear transport receptor between the nucleus and cytoplasm, the human XPO1/CRM1 protein is preferentially localized at the nuclear envelope in interphase cells (Kudo et al., 1997; Fornerod et al., 1997b). In the nucleus it can be detected in specific bodies called CRM1 nucleolar bodies (CNoBs). CNoBs depend on RNA polymerase I activity, suggesting a role in ribosome biogenesis (Ernoult-Lange et al., 2009).
In mitotic cells, a fraction of XPO1 is found at centrosomes (Forgues et al., 2003; Wang et al., 2005) and a substantial fraction localizes to the kinetochores (Arnaoutov et al., 2005).
  The plates show the subcellular localisation of CRM1 (detected by indirect immunofluorescence) in interphase and mitotic human HeLa cells. Upper row: an interphase cell showing CRM1 (in red in the left panel) within the nucleus and especially around the nuclear envelope, where it concentrates with a regular, punctuated pattern typical of the association with nuclear pore complexes. The nuclear shape is depicted in the upper right panel by staining the DNA with the fluorochrome 4',6-diamidino-2-phenylindole (DAPI, in blue). Lower row: a metaphase cell showing CRM1 (in red in the left panel) concentrating at the kinetochores (compare with the middle panel, where kinetochore proteins are stained using CREST antiserum and a blue-emitting secondary antibody). A CRM1 fraction is also visible at spindle poles (compare with the staining of the mitotic spindle microtubules using an antibody against alpha-tubulin, in green). The merged picture shows a 3.5x magnification of the overlay of all three images: CRM1 (red) lies at the interface between the kinetochores (blue) and the microtubules (green) projecting from opposite spindle poles.
Function hCRM1 was found to interact stably in complexes containing not only NUP214/CAN (or its derivatives), but also another component of nuclear pores, the nucleoporin NUP88 (Fornerod et al., 1997b). These interactions hinted at a possible role of hCRM1 in nucleocytoplasmic transport. Further studies indeed demonstrated that hCRM1 acts as a nuclear export factor (reviewed by Fried and Kutaj, 2003; Hutten and Kehlenbach, 2007): it interacts with various classes of RNAs and with proteins carrying nuclear export signals (NES) (Fornerod et al., 1997c; Fukuda et al., 1997; Ossareh-Nazari et al., 1997), short aminoacidic stretches harbouring hydrophobic residues (general consensus LX(2-3)ΦX(2-3)LXΦ, where can be L, I, M or F), present in many shuttling proteins of cellular or viral origin, and transports these molecules out of the nucleus through nuclear pore complexes in a manner dependent on the GTPase RAN. The protein is therefore alternatively called either exportin-1 or XPO1, based on its function, or hCRM1, based on evolutionary conservation.
Regulated export of some shuttling proteins (e.g., p53, p27, STAT, NF-kB and many viral proteins) out of the nucleus is essential for regulated cell cycle and cell proliferation (reviewed by Fabbro and Henderson, 2003; Rensen et al., 2008). This has lead some authors to view nuclear export as a promising target process in cancer therapy (reviewed by Yashiroda and Yoshida, 2003; Turner and Sullivan, 2008).
Recent findings have revealed additional roles of XPO1/CRM1 in mitosis: first, an XPO1/CRM1 fraction regulates the localisation of nucleophosmin (NPM/B23), a regulator of centrosome duplication. XPO1/CRM1 is required to prevent centrosome overduplication and the formation of multipolar spindles (reviewed by Budhu and Wang, 2005; Ciciarello and Lavia, 2005). Second, a kinetochore-associated fraction of XPO1/CRM1 regulates the assembly of the so-called k-fibers, bundles of microtubules that stably connect the spindle poles to the kinetochores of mitotic chromosomes to ensure proper chromosome segregation (reviewed by Arnaoutov and Dasso, 2005; Ciciarello and Lavia, 2005; Dasso, 2006). Third, XPO1/CRM1 regulates survivin, a member of the chromosomal passenger complex with roles in chromosome segregation and apoptosis (reviewed by Knauer et al., 2007).
In synthesis, XPO1/CRM1 acts in control of cell proliferation, and affects loss of proliferation control in cancer cells, through several pathways: 1. as a nuclear export factor, it directly regulates the subcellular localisation, and hence the activity, of oncogenes and tumour suppressor proteins that contain nuclear export sequences; 2. it acts in control of the mitotic apparatus and chromosome segregation; 3. it influences the maintenance of nuclear and chromosome structure.
Homology The human protein originally named CC112 showed homology to the Schizosaccharomyces pombe CRM1 protein, first identified for being implicated in the control of higher order chromosome structure: mutation of the coding gene was associated with the appearance of "deformed nuclear chromosome domains" in fission yeast conditional mutant strains. The gene product was therefore named CRM1 (chromosome region maintenance 1; Adachi and Yanagida, 1989). Based on this homology, the human protein name of CC112 was abandoned and the name hCRM1 was used.

Implicated in

Entity Ovarian cancer (Noske et al., 2008)
Prognosis Increased nuclear (52.7%) and cytoplasmic (56.8%) expression of CRM1 were reported observed in carcinomas compared with borderline tumors and benign lesions. Cytoplasmic CRM1 expression significantly correlated with advanced tumor stage (P= 0.043), poorly differentiated carcinomas (P= 0.011) and high mitotic rate (P= 0.008). Nuclear CRM1 was significantly associated with high cyclooxygenase-2 (COX-2) expression (P= 0.002) and poor overall survival (P= 0.01). CRM1 was previously directly implicated in nuclear export of COX-2 (Jang et al., 2003). The study by Noske et al. (2008) suggests that elevated expression of CRM1 may be causal to COX-2 up-regulation, with direct clinical relevance.
Oncogenesis CRM1 is highly expressed in ovarian carcinomas tissues and regulates export of COX-2.
Entity Osteosarcoma (Yao et al., 2009)
Prognosis The CRM1 protein is reported to be expressed with increased abundance in osteosarcoma compared to non-tumour tissues (P= 0.037, 57 patients). High levels of CRM1 were significantly associated with increased serum levels of alkaline phosphatase (ALP, P= 0.001). In univariate analysis, a significant association between CRM1 expression and tumor size (P= 0.014), as well as histological grade (P= 0.003) was observed. In Kaplan-Meier survival analysis, high CRM1 expression was a significant prognostic indicator for poor progression-free survival (P= 0.016) as well as overall survival (P= 0.008). Multivariate analysis demonstrated that high expression of CRM1 was significantly related to shorter survival (95% CI, 1.27-5.39).
Oncogenesis CRM1 is significantly increased in osteosarcoma compared with normal tissue.
Entity Cervical cancer (van der Watt et al., 2009)
Oncogenesis CRM1 protein abundance is significantly increased in cervical cancer cells compared with normal tissue (P< 0.05). Inhibition of CRM1 by RNA interference resulted in increased cell death, associated with nuclear retention of p53, likely protecting p53 from degradation as the latter predominantly occurs in the cytoplasm.
Entity Pancreas cancer (Huang et al., 2009)
Prognosis Increased expression abundance of CRM1 protein was detected in pancreatic cancer tissues (P= 0.0013, 69 patients at stages I and II). CRM1 expression correlates with increased levels of serum CEA (P= 0.002) and CA19.9 (P= 0.005), tumour size (P= 0.011), lymphadenopathy (P= 0.004) and metastasis (P= 0.0041). High CRM1 expression was a prognostic indicator for progression-free survival (PFS) (P= 0.0011) as well as overall survival (OS) (P= 0.004). The authors proposed that CRM1 be used as a prognostic parameter for poor PFS and OS (95% CI, 1.27-5.39).
Entity Glioma (Shen et al., 2009)
Prognosis CRM1 overexpression is significantly associated with the pathological state (P= 0.001, 56 patients), with glioma tumour grade, with high expression of phospho-ser10p27 and with reduced overall abundance of p27.
Oncogenesis Given the direct implication of CRM1 in nuclear export of p27, the data in this study suggest that increased CRM1 abundance yields increased cytoplasmic localisation of p27, which is probably targeted to degradation, leading to uncontrolled tumour growth. Phospho-ser10p27 may be resistant to CRM1-mediated nuclear export. High CRM1 and low p27 expression are associated with high grade glioma and high CRM1 protein expression is proposed as a prognostic factor of overall survival and poor outcome.

To be noted

CRM1 protein levels are abnormally high in several cancers, with high levels of CRM1 being associated with poor patient survival (van der Watt and Leaner, 2011).

External links

HGNC (Hugo)XPO1   12825
Entrez_Gene (NCBI)XPO1  7514  exportin 1
GeneCards (Weizmann)XPO1
Ensembl hg19 (Hinxton)ENSG00000082898 [Gene_View]  chr2:61705069-61765418 [Contig_View]  XPO1 [Vega]
Ensembl hg38 (Hinxton)ENSG00000082898 [Gene_View]  chr2:61705069-61765418 [Contig_View]  XPO1 [Vega]
ICGC DataPortalENSG00000082898
AceView (NCBI)XPO1
Genatlas (Paris)XPO1
SOURCE (Princeton)XPO1
Genomic and cartography
GoldenPath hg19 (UCSC)XPO1  -     chr2:61705069-61765418 -  2p15   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)XPO1  -     2p15   [Description]    (hg38-Dec_2013)
EnsemblXPO1 - 2p15 [CytoView hg19]  XPO1 - 2p15 [CytoView hg38]
Mapping of homologs : NCBIXPO1 [Mapview hg19]  XPO1 [Mapview hg38]
Gene and transcription
Genbank (Entrez)AK094339 AK124769 AK289920 AK299039 AK312426
RefSeq transcript (Entrez)NM_003400
RefSeq genomic (Entrez)NC_000002 NC_018913 NT_022184 NW_004929300
Consensus coding sequences : CCDS (NCBI)XPO1
Cluster EST : UnigeneHs.370770 [ NCBI ]
CGAP (NCI)Hs.370770
Alternative Splicing : Fast-db (Paris)GSHG0017651
Alternative Splicing GalleryENSG00000082898
Gene ExpressionXPO1 [ NCBI-GEO ]     XPO1 [ SEEK ]   XPO1 [ MEM ]
SOURCE (Princeton)Expression in : [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO14980 (Uniprot)
NextProtO14980  [Medical]
With graphics : InterProO14980
Splice isoforms : SwissVarO14980 (Swissvar)
Domaine pattern : Prosite (Expaxy)IMPORTIN_B_NT (PS50166)   
Domains : Interpro (EBI)ARM-like    ARM-type_fold    CRM1_C_dom    Exportin-1/Importin-b-like    Importin-beta_N   
Related proteins : CluSTrO14980
Domain families : Pfam (Sanger)CRM1_C (PF08767)    IBN_N (PF03810)    Xpo1 (PF08389)   
Domain families : Pfam (NCBI)pfam08767    pfam03810    pfam08389   
Domain families : Smart (EMBL)CRM1_C (SM01102)  IBN_N (SM00913)  
DMDM Disease mutations7514
Blocks (Seattle)O14980
PDB (SRS)1W9C    2L1L    3GB8    4BSM    4BSN   
PDB (PDBSum)1W9C    2L1L    3GB8    4BSM    4BSN   
PDB (IMB)1W9C    2L1L    3GB8    4BSM    4BSN   
PDB (RSDB)1W9C    2L1L    3GB8    4BSM    4BSN   
Human Protein AtlasENSG00000082898
Peptide AtlasO14980
IPIIPI00298961   IPI00892777   IPI00892935   IPI00892827   IPI00894253   IPI00894165   IPI00894059   IPI00893889   IPI00893771   IPI00893403   
Protein Interaction databases
IntAct (EBI)O14980
Ontologies - Pathways
Ontology : AmiGOribosomal large subunit export from nucleus  ribosomal small subunit export from nucleus  negative regulation of transcription from RNA polymerase II promoter  mitotic cell cycle  kinetochore  RNA binding  transporter activity  nucleocytoplasmic transporter activity  protein binding  nucleus  nuclear envelope  annulate lamellae  nucleoplasm  nucleoplasm  nucleolus  cytoplasm  cytosol  protein export from nucleus  transforming growth factor beta receptor signaling pathway  Ran GTPase binding  protein transporter activity  gene expression  regulation of centrosome duplication  Cajal body  membrane  viral process  viral life cycle  protein domain specific binding  negative regulation of transforming growth factor beta receptor signaling pathway  ribonucleoprotein complex  nuclear membrane  protein localization to nucleus  regulation of protein catabolic process  response to drug  intracellular membrane-bounded organelle  regulation of protein export from nucleus  mRNA transport  intracellular transport of virus  
Ontology : EGO-EBIribosomal large subunit export from nucleus  ribosomal small subunit export from nucleus  negative regulation of transcription from RNA polymerase II promoter  mitotic cell cycle  kinetochore  RNA binding  transporter activity  nucleocytoplasmic transporter activity  protein binding  nucleus  nuclear envelope  annulate lamellae  nucleoplasm  nucleoplasm  nucleolus  cytoplasm  cytosol  protein export from nucleus  transforming growth factor beta receptor signaling pathway  Ran GTPase binding  protein transporter activity  gene expression  regulation of centrosome duplication  Cajal body  membrane  viral process  viral life cycle  protein domain specific binding  negative regulation of transforming growth factor beta receptor signaling pathway  ribonucleoprotein complex  nuclear membrane  protein localization to nucleus  regulation of protein catabolic process  response to drug  intracellular membrane-bounded organelle  regulation of protein export from nucleus  mRNA transport  intracellular transport of virus  
Pathways : BIOCARTASonic Hedgehog (SHH) Receptor Ptc1 Regulates cell cycle [Genes]    Regulation of Spermatogenesis by CREM [Genes]   
Pathways : KEGGRibosome biogenesis in eukaryotes    RNA transport    Influenza A    HTLV-I infection    Epstein-Barr virus infection   
REACTOMEO14980 [protein]
REACTOME PathwaysREACT_115566 Cell Cycle [pathway]
REACTOME PathwaysREACT_116125 Disease [pathway]
REACTOME PathwaysREACT_71 Gene Expression [pathway]
REACTOME PathwaysREACT_21257 Metabolism of RNA [pathway]
REACTOME PathwaysREACT_21300 Mitotic M-M/G1 phases [pathway]
REACTOME PathwaysREACT_111102 Signal Transduction [pathway]
Protein Interaction DatabaseXPO1
DoCM (Curated mutations)XPO1
Wikipedia pathwaysXPO1
Gene fusion - rearrangements
Polymorphisms : SNP, variants
NCBI Variation ViewerXPO1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)XPO1
Exome Variant ServerXPO1
SNP (GeneSNP Utah)XPO1
Genetic variants : HAPMAPXPO1
Genomic Variants (DGV)XPO1 [DGVbeta]
ICGC Data PortalENSG00000082898 
Cancer Gene: CensusXPO1 
Somatic Mutations in Cancer : COSMICXPO1 
CONAN: Copy Number AnalysisXPO1 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
DECIPHER (Syndromes)2:61705069-61765418
Mutations and Diseases : HGMDXPO1
NextProtO14980 [Medical]
Disease Genetic AssociationXPO1
Huge Navigator XPO1 [HugePedia]  XPO1 [HugeCancerGEM]
snp3D : Map Gene to Disease7514
DGIdb (Drug Gene Interaction db)XPO1
General knowledge
Homologs : HomoloGeneXPO1
Homology/Alignments : Family Browser (UCSC)XPO1
Phylogenetic Trees/Animal Genes : TreeFamXPO1
Chemical/Protein Interactions : CTD7514
Chemical/Pharm GKB GenePA37418
Clinical trialXPO1
Cancer Resource (Charite)ENSG00000082898
Other databases
Other databaseModBase
Other databasePhylomeDB
Other database
PubMed315 Pubmed reference(s) in Entrez


Higher order chromosome structure is affected by cold-sensitive mutations in a Schizosaccharomyces pombe gene crm1+ which encodes a 115-kD protein preferentially localized in the nucleus and its periphery.
Adachi Y, Yanagida M.
J Cell Biol. 1989 Apr;108(4):1195-207.
PMID 2647765
The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA.
von Lindern M, Fornerod M, van Baal S, Jaegle M, de Wit T, Buijs A, Grosveld G.
Mol Cell Biol. 1992 Apr;12(4):1687-97.
PMID 1549122
Interaction of cellular proteins with the leukemia specific fusion proteins DEK-CAN and SET-CAN and their normal counterpart, the nucleoporin CAN.
Fornerod M, Boer J, van Baal S, Morreau H, Grosveld G.
Oncogene. 1996 Oct 17;13(8):1801-8.
PMID 8895527
Chromosomal localization of genes encoding CAN/Nup214-interacting proteins--human CRM1 localizes to 2p16, whereas Nup88 localizes to 17p13 and is physically linked to SF2p32.
Fornerod M, van Baal S, Valentine V, Shapiro DN, Grosveld G.
Genomics. 1997a Jun 15;42(3):538-40.
PMID 9205132
The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88.
Fornerod M, van Deursen J, van Baal S, Reynolds A, Davis D, Murti KG, Fransen J, Grosveld G.
EMBO J. 1997b Feb 17;16(4):807-16.
PMID 9049309
CRM1 is an export receptor for leucine-rich nuclear export signals.
Fornerod M, Ohno M, Yoshida M, Mattaj IW.
Cell. 1997c Sep 19;90(6):1051-60.
PMID 9323133
CRM1 is responsible for intracellular transport mediated by the nuclear export signal.
Fukuda M, Asano S, Nakamura T, Adachi M, Yoshida M, Yanagida M, Nishida E.
Nature. 1997 Nov 20;390(6657):308-11.
PMID 9384386
Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins.
Kudo N, Khochbin S, Nishi K, Kitano K, Yanagida M, Yoshida M, Horinouchi S.
J Biol Chem. 1997 Nov 21;272(47):29742-51.
PMID 9368044
Evidence for a role of CRM1 in signal-mediated nuclear protein export.
Ossareh-Nazari B, Bachelerie F, Dargemont C.
Science. 1997 Oct 3;278(5335):141-4.
PMID 9311922
Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA.
Wolff B, Sanglier JJ, Wang Y.
Chem Biol. 1997 Feb;4(2):139-47.
PMID 9190288
Regulation of tumor suppressors by nuclear-cytoplasmic shuttling.
Fabbro M, Henderson BR.
Exp Cell Res. 2003 Jan 15;282(2):59-69. (REVIEW)
PMID 12531692
Involvement of Crm1 in hepatitis B virus X protein-induced aberrant centriole replication and abnormal mitotic spindles.
Forgues M, Difilippantonio MJ, Linke SP, Ried T, Nagashima K, Feden J, Valerie K, Fukasawa K, Wang XW.
Mol Cell Biol. 2003 Aug;23(15):5282-92.
PMID 12861014
Nucleocytoplasmic transport: taking an inventory.
Fried H, Kutay U.
Cell Mol Life Sci. 2003 Aug;60(8):1659-88. (REVIEW)
PMID 14504656
Leptomycin B, an inhibitor of the nuclear export receptor CRM1, inhibits COX-2 expression.
Jang BC, Munoz-Najar U, Paik JH, Claffey K, Yoshida M, Hla T.
J Biol Chem. 2003 Jan 31;278(5):2773-6. Epub 2002 Dec 4.
PMID 12468543
Nucleo-cytoplasmic transport of proteins as a target for therapeutic drugs.
Yashiroda Y, Yoshida M.
Curr Med Chem. 2003 May;10(9):741-8. (REVIEW)
PMID 12678777
Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.
Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-Lopez M, Baudin F, Mattaj IW, Muller CW.
Mol Cell. 2004 Dec 3;16(5):761-75.
PMID 15574331
Crm1 is a mitotic effector of Ran-GTP in somatic cells.
Arnaoutov A, Azuma Y, Ribbeck K, Joseph J, Boyarchuk Y, Karpova T, McNally J, Dasso M.
Nat Cell Biol. 2005 Jun;7(6):626-32.
PMID 15908946
Ran-GTP regulates kinetochore attachment in somatic cells.
Arnaoutov A, Dasso M.
Cell Cycle. 2005 Sep;4(9):1161-5. Epub 2005 Sep 28. (REVIEW)
PMID 16082212
Loading and unloading: orchestrating centrosome duplication and spindle assembly by Ran/Crm1.
Budhu AS, Wang XW.
Cell Cycle. 2005 Nov;4(11):1510-4. Epub 2005 Nov 20. (REVIEW)
PMID 16294017
New CRIME plots. Ran and transport factors regulate mitosis.
Ciciarello M, Lavia P.
EMBO Rep. 2005 Aug;6(8):714-6. (REVIEW)
PMID 16065064
Temporal and spatial control of nucleophosmin by the Ran-Crm1 complex in centrosome duplication.
Wang W, Budhu A, Forgues M, Wang XW.
Nat Cell Biol. 2005 Aug;7(8):823-30. Epub 2005 Jul 24.
PMID 16041368
Ran at kinetochores.
Dasso M.
Biochem Soc Trans. 2006 Nov;34(Pt 5):711-5.
PMID 17052180
CRM1-mediated nuclear export: to the pore and beyond.
Hutten S, Kehlenbach RH.
Trends Cell Biol. 2007 Apr;17(4):193-201. Epub 2007 Feb 20.
PMID 17317185
Survivin's dual role: an export's view.
Knauer SK, Mann W, Stauber RH.
Cell Cycle. 2007 Mar 1;6(5):518-21. Epub 2007 Mar 21. (REVIEW)
PMID 17361097
Expression of the nuclear export protein chromosomal region maintenance/exportin 1/Xpo1 is a prognostic factor in human ovarian cancer.
Noske A, Weichert W, Niesporek S, Roske A, Buckendahl AC, Koch I, Sehouli J, Dietel M, Denkert C.
Cancer. 2008 Apr 15;112(8):1733-43.
PMID 18306389
The GTPase Ran: regulation of cell life and potential roles in cell transformation.
Rensen WM, Mangiacasale R, Ciciarello M, Lavia P.
Front Biosci. 2008 May 1;13:4097-121. (REVIEW)
PMID 18508502
CRM1-mediated nuclear export of proteins and drug resistance in cancer.
Turner JG, Sullivan DM.
Curr Med Chem. 2008;15(26):2648-55. (REVIEW)
PMID 18991627
Nucleocytoplasmic traffic of CPEB1 and accumulation in Crm1 nucleolar bodies.
Ernoult-Lange M, Wilczynska A, Harper M, Aigueperse C, Dautry F, Kress M, Weil D.
Mol Biol Cell. 2009 Jan;20(1):176-87. Epub 2008 Oct 15.
PMID 18923137
Prognostic value of CRM1 in pancreas cancer.
Huang WY, Yue L, Qiu WS, Wang LW, Zhou XH, Sun YJ.
Clin Invest Med. 2009 Dec 1;32(6):E315.
PMID 20003838
Expression of CRM1 in human gliomas and its significance in p27 expression and clinical prognosis.
Shen A, Wang Y, Zhao Y, Zou L, Sun L, Cheng C.
Neurosurgery. 2009 Jul;65(1):153-9; discussion 159-60.
PMID 19574837
The Karyopherin proteins, Crm1 and Karyopherin beta1, are overexpressed in cervical cancer and are critical for cancer cell survival and proliferation.
van der Watt PJ, Maske CP, Hendricks DT, Parker MI, Denny L, Govender D, Birrer MJ, Leaner VD.
Int J Cancer. 2009 Apr 15;124(8):1829-40.
PMID 19117056
The expression of CRM1 is associated with prognosis in human osteosarcoma.
Yao Y, Dong Y, Lin F, Zhao H, Shen Z, Chen P, Sun YJ, Tang LN, Zheng SE.
Oncol Rep. 2009 Jan;21(1):229-35.
PMID 19082467
NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.
Guttler T, Madl T, Neumann P, Deichsel D, Corsini L, Monecke T, Ficner R, Sattler M, Gorlich D.
Nat Struct Mol Biol. 2010 Nov;17(11):1367-76. Epub 2010 Oct 24.
PMID 20972448
The nuclear exporter, Crm1, is regulated by NFY and Sp1 in cancer cells and repressed by p53 in response to DNA damage.
van der Watt PJ, Leaner VD.
Biochim Biophys Acta. 2011 Jul;1809(7):316-26. Epub 2011 Jun 13.
PMID 21683812
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Written11-2011Alessandra Ruggiero, Maria Giubettini, Patrizia Lavia
CNR (National Research Council), Institute of Molecular Biology and Pathology, c/o Sapienza University of Rome, via degli Apuli 4, 00185 Rome, Italy


This paper should be referenced as such :
Ruggiero, A ; Giubettini, M ; Lavia, P
XPO1 (exportin 1 (CRM1 homolog, yeast))
Atlas Genet Cytogenet Oncol Haematol. 2012;16(3):228-232.
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