Atlas of Genetics and Cytogenetics in Oncology and Haematology


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PLK1 (polo-like kinase 1 (Drosophila))

Identity

Other namesPLK
STPK13 (SERINE/THREONINE PROTEIN KINASE 13)
HGNC (Hugo) PLK1
LocusID (NCBI) 5347
Location 16p12.2
Location_base_pair Starts at 23690201 and ends at 23701688 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order Genes flanking PLK1 in centromere to telomere direction on 16p12 are:
  • UBPH, 16p12, similar to ubiquitin binding protein
  • NDUFAB1, 16p12.1, NADH dehydrogenase (ubiquinone) 1, alpha/beta subcomplex, 1,8kDa
  • FLJ21816, 16p12.1, hypothetical protein FLJ21816
  • MGC3248, 16p12.1, dynactin 4
  • PLK1, 16p12.1, polo-like kinase 1 (Drosophila)
  • LOC388226, 16p12.1, similar to endoplasmic reticulum (ER) to nucleus signaling 2; inositol-requiring 1 (Yeast homologue)
  • LOC63928, 16p12.1, hepatocellular carcinoma antigen gene 520
  • PRKCB1, 16p11.2, protein kinase C, beta 1
  • CACNG3, 16p12-p13.1, calcium channel, voltage-dependent, gamma subunit 3
  • Note Polo like kinases belong to serine/threonine kinases that are conserved from yeast to human cells. Polo like kinases exhibit important roles in key cellular events regulating cell cycle progression and cell division such as centrosome maturation, cdc2 activation, mitotic spindle formation, regulation of the anaphase promoting complex, chromosome segregation, cytokinesis, DNA damage response pathways and apoptosis.

    DNA/RNA

     
      The alignment of PLK1 mRNA (NM_005030) to its genomic sequence NC_000016).
    Description PLK1 mRNA spans approximately 11.5 kb and has 10 exons. The sizes of the exons 1 to 10 are 461, 169, 145, 94, 220, 156, 78, 155, 183 and 508 bps.
    Transcription PLK1 mRNA (NM_005030) is 2204 bp. PLK1 expression is believed to reach its peak value in mitosis in the cell cycle. It is highly expressed in actively proliferating tissues such as those in the placenta, spleen, ovary, and testis. High expression of PLK1 is also detected in various neoplastic tissues. Northern blot analysis reveals low or undetectable levels of PLK1 transcript in most other adult tissues (e.g.: brain, thymus, liver, lung, pancreas, heart, kidney, stomach, intestine and skin).
    Pseudogene Mouse Plk gene maps to Chromosome 7 and the processed pseudogene to mouse Chromosome 5. No human pseudogene for PLK1 has been reported.

    Protein

    Description Protein consists of 603 amino acids and is 66kDa. In addition to the N-terminus kinase domain, there are two conserved polo-box regions of 30 amino acids at the C-terminus. Kinase activity is regulated at least in part, by the polo-boxes that are functionally important for both auto-inhibition and sub-cellular localization.
    Expression PLK1 protein becomes a target of the anaphase-promoting complex/cyclosome and is degraded by the ubiquitin-proteasome pathway as cells exit mitosis.
    Localisation During interphase, PLK1 localizes to centrosomes. In early mitosis, it associates with mitotic spindle poles. A recombinant GFP-PLK1 protein localizes to centromere/kinetochore region, suggesting a possible role for chromosome separation.
    Function PLK1 is believed to be involved in the regulation of key steps during cell division, DNA damage repair pathways, apoptosis, and the progression of the cell cycle.
    PLK1 has roles in the activation of cdc2 through cdc25 and direct phosphorylation of cyclin B1, through which MPF (mitosis promoting factor) is activated so that mitosis can start.
    Microinjection of PLK1 antibodies causes failure of g-tubulin recruitment to the centrosomes. This failure results in immature centrosomes and monopolar spindle formation. Similar microinjection experiments in cell lines (transformed HeLa and non-immortalized Hs68 fibroblasts) result in a marked inhibition of cell cycle progression.
    PLK1 also has a possible role during cytokinesis based on the observation that PLK1 interacts and co-localizes with a kinesin related motor protein (CHO1/MKLP-1) at the interzone during anaphase and the mid-body during telophase and cytokinesis.
    Evidence suggests that BRCA2 is a substrate of PLK1 both in response to DNA damage and during normal cell cycle progression. This suggests a role for PLK1 in regulating DNA damage repair.
    Other studies have shown that the loss of PLK1 expression can induce pro-apoptotic pathways and inhibit growth.
    Based on yeast and murine studies of meiosis, human PLK1 may also have a regulatory function in meiosis. S. cerevisiae polo kinase CDC5 is required to phosphorylate and remove meiotic cohesion during the first cell division. In CDC5 depleted cells, kinetochores are bioriented during meiosis I, and Mam1, a protein essential for coorientation, fails to associate with kinetochores. CDC5 is believed to have roles in sister-kinetochore coorientation and chromosome segregation during meiosis I..
    Homology P.troglodytes: PLK1, polo-like kinase, XP_510879.1, 735 aa
    M.musculus: Plk1, polo-like kinase 1 (Drosophila), NP_035251.2, 603 aa
    R.norvegicus: Plk1, polo-like kinase 1 (Drosophila), NP_058796.1, 603 aa
    D.melanogaster: polo, polo, NP_524179.2, 576 aa
    C.elegans: plk-1 PoLo Kinase, NP_741243.1, 649 aa
    S.cerevisiae: CDC5, NP_013714.1, 705 aa

    Implicated in

    Note Increased PLK1 levels are detected in a variety of cancers.
    Disease Increased PLK1 transcript has been detected in a variety of tumor types including esophageal, head and neck squamous cell, liver, lung and breast carcinomas. Immunohistochemical studies also demonstrate increased PLK1 protein levels in melanomas, breast, ovarian, prostate cancers, and head, neck squamous cell carcinomas.
    Prognosis Statistically significant correlations between increased PLK1 expression and decreased patient survival suggest that PLK1 is a negative prognostic indicator for some types of cancer. For example,
  • In prostate cancer, PLK1 overexpression is linked to higher tumor grades
  • In non-Hodgkin's lymphomas, PLK1 overexpression reflect malignancy potentials
  • In hepatoblastomas, ovarian, colorectal cancers and melanomas, PLK1 overexpression suggests PLK1 to be a poor-prognostic indicator.
  • Oncogenesis Oncogenic properties of PLK1 are believed to be due to its role in driving cell cycle progression. Supporting evidence comes from the overexpression studies of PLK1 in NIH3T3 cell line. These cells become capable of forming foci and growing in soft agar and more importantly, these cells can form tumors in nude mice due to PLK1 overexpression.

    PLK1 has also been linked to known pathways that are altered during the neoplastic transformation. Retinoblastoma tumor suppressor (RB) pathway activation results in the repression of PLK1 promoter in a SWI/SNF chromatin remodeling complex dependent manner. In case of RB inactivation, PLK1 expression seems to be deregulated. This new finding suggests that PLK1 may be a target of the retinoblastoma tumor suppressor (RB) pathway.

    Moreover, PLK1 seems to be involved in the tumor suppressor p53 related pathways. Evidence suggests that PLK1 can inhibit transactivation and pro-apoptotic functions of p53 function by physical interaction and phosphorylation.

    In addition to PLK1šs role in normal cell cycle regulation, its connection to such known tumor suppressors may be crucial for the tumorigenesis processes.

      

    To be noted

    A study also suggests that PLK1 protein cannot be detected in normal brain tissue but it can be detected in brain tissues from Alzheimeršs disease patients.

    External links

    Nomenclature
    HGNC (Hugo)PLK1   9077
    Cards
    AtlasPLK1ID41747ch16p12
    Entrez_Gene (NCBI)PLK1  5347  polo-like kinase 1
    GeneCards (Weizmann)PLK1
    Ensembl (Hinxton)ENSG00000166851 [Gene_View]  chr16:23690201-23701688 [Contig_View]  PLK1 [Vega]
    ICGC DataPortalENSG00000166851
    AceView (NCBI)PLK1
    Genatlas (Paris)PLK1
    WikiGenes5347
    SOURCE (Princeton)NM_005030
    Genomic and cartography
    GoldenPath (UCSC)PLK1  -  16p12.2   chr16:23690201-23701688 +  16p   [Description]    (hg19-Feb_2009)
    EnsemblPLK1 - 16p [CytoView]
    Mapping of homologs : NCBIPLK1 [Mapview]
    OMIM602098   
    Gene and transcription
    Genbank (Entrez)AB084459 AB209179 AK303263 AK308276 AK313227
    RefSeq transcript (Entrez)NM_005030
    RefSeq genomic (Entrez)AC_000148 NC_000016 NC_018927 NT_187260 NW_001838401 NW_004929400
    Consensus coding sequences : CCDS (NCBI)PLK1
    Cluster EST : UnigeneHs.592049 [ NCBI ]
    CGAP (NCI)Hs.592049
    Alternative Splicing : Fast-db (Paris)GSHG0011042
    Alternative Splicing GalleryENSG00000166851
    Gene ExpressionPLK1 [ NCBI-GEO ]     PLK1 [ SEEK ]   PLK1 [ MEM ]
    Protein : pattern, domain, 3D structure
    UniProt/SwissProtP53350 (Uniprot)
    NextProtP53350  [Medical]
    With graphics : InterProP53350
    Splice isoforms : SwissVarP53350 (Swissvar)
    Catalytic activity : Enzyme2.7.11.21 [ Enzyme-Expasy ]   2.7.11.212.7.11.21 [ IntEnz-EBI ]   2.7.11.21 [ BRENDA ]   2.7.11.21 [ KEGG ]   
    Domaine pattern : Prosite (Expaxy)POLO_BOX (PS50078)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_ST (PS00108)   
    Domains : Interpro (EBI)Kinase-like_dom    POLO_box_duplicated_dom    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser/Thr_dual-sp_kinase_dom    Ser/Thr_kinase_AS   
    Related proteins : CluSTrP53350
    Domain families : Pfam (Sanger)Pkinase (PF00069)    POLO_box (PF00659)   
    Domain families : Pfam (NCBI)pfam00069    pfam00659   
    Domain families : Smart (EMBL)S_TKc (SM00220)  
    DMDM Disease mutations5347
    Blocks (Seattle)P53350
    PDB (SRS)1Q4K    1Q4O    1UMW    2OGQ    2OJX    2OU7    2OWB    2RKU    2V5Q    2YAC    3BZI    3C5L    3FC2    3FVH    3HIH    3HIK    3KB7    3P2W    3P2Z    3P34    3P35    3P36    3P37    3Q1I    3RQ7    3THB    4A4L    4A4O    4DFW    4E67    4E9C    4E9D    4H5X    4H71    4HAB    4HCO    4HY2    4J52    4J53    4LKL    4LKM    4MLU   
    PDB (PDBSum)1Q4K    1Q4O    1UMW    2OGQ    2OJX    2OU7    2OWB    2RKU    2V5Q    2YAC    3BZI    3C5L    3FC2    3FVH    3HIH    3HIK    3KB7    3P2W    3P2Z    3P34    3P35    3P36    3P37    3Q1I    3RQ7    3THB    4A4L    4A4O    4DFW    4E67    4E9C    4E9D    4H5X    4H71    4HAB    4HCO    4HY2    4J52    4J53    4LKL    4LKM    4MLU   
    PDB (IMB)1Q4K    1Q4O    1UMW    2OGQ    2OJX    2OU7    2OWB    2RKU    2V5Q    2YAC    3BZI    3C5L    3FC2    3FVH    3HIH    3HIK    3KB7    3P2W    3P2Z    3P34    3P35    3P36    3P37    3Q1I    3RQ7    3THB    4A4L    4A4O    4DFW    4E67    4E9C    4E9D    4H5X    4H71    4HAB    4HCO    4HY2    4J52    4J53    4LKL    4LKM    4MLU   
    PDB (RSDB)1Q4K    1Q4O    1UMW    2OGQ    2OJX    2OU7    2OWB    2RKU    2V5Q    2YAC    3BZI    3C5L    3FC2    3FVH    3HIH    3HIK    3KB7    3P2W    3P2Z    3P34    3P35    3P36    3P37    3Q1I    3RQ7    3THB    4A4L    4A4O    4DFW    4E67    4E9C    4E9D    4H5X    4H71    4HAB    4HCO    4HY2    4J52    4J53    4LKL    4LKM    4MLU   
    Human Protein AtlasENSG00000166851
    Peptide AtlasP53350
    HPRD03652
    IPIIPI00021248   IPI00556429   IPI00455896   
    Protein Interaction databases
    DIP (DOE-UCLA)P53350
    IntAct (EBI)P53350
    FunCoupENSG00000166851
    BioGRIDPLK1
    IntegromeDBPLK1
    STRING (EMBL)PLK1
    Ontologies - Pathways
    QuickGOP53350
    Ontology : AmiGOmitotic sister chromatid segregation  G2/M transition of mitotic cell cycle  G2/M transition of mitotic cell cycle  negative regulation of transcription from RNA polymerase II promoter  mitotic cell cycle  mitotic cytokinesis  kinetochore  cytokinesis  cytokinesis  spindle pole  condensed nuclear chromosome outer kinetochore  microtubule bundle formation  protein kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein binding  ATP binding  nucleus  nucleoplasm  nucleolus  cytoplasm  centrosome  spindle  cytosol  spindle microtubule  protein phosphorylation  mitotic nuclear division  mitotic nuclear division  mitotic nuclear envelope disassembly  metaphase/anaphase transition of mitotic cell cycle  activation of mitotic anaphase-promoting complex activity  mitotic spindle assembly checkpoint  regulation of mitotic cell cycle  microtubule binding  cell proliferation  positive regulation of peptidyl-threonine phosphorylation  anaphase-promoting complex binding  microtubule cytoskeleton  kinase activity  protein ubiquitination  peptidyl-serine phosphorylation  protein kinase binding  regulation of mitotic metaphase/anaphase transition  midbody  anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process  G2 DNA damage checkpoint  protein destabilization  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  polar body extrusion after meiotic divisions  negative regulation of apoptotic process  regulation of protein binding  establishment of protein localization  negative regulation of cyclin-dependent protein serine/threonine kinase activity  positive regulation of proteolysis  response to antibiotic  spindle midzone  centrosome organization  positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle  regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle  positive regulation of ubiquitin-protein transferase activity  regulation of cell cycle  protein localization to chromatin  
    Ontology : EGO-EBImitotic sister chromatid segregation  G2/M transition of mitotic cell cycle  G2/M transition of mitotic cell cycle  negative regulation of transcription from RNA polymerase II promoter  mitotic cell cycle  mitotic cytokinesis  kinetochore  cytokinesis  cytokinesis  spindle pole  condensed nuclear chromosome outer kinetochore  microtubule bundle formation  protein kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein serine/threonine kinase activity  protein binding  ATP binding  nucleus  nucleoplasm  nucleolus  cytoplasm  centrosome  spindle  cytosol  spindle microtubule  protein phosphorylation  mitotic nuclear division  mitotic nuclear division  mitotic nuclear envelope disassembly  metaphase/anaphase transition of mitotic cell cycle  activation of mitotic anaphase-promoting complex activity  mitotic spindle assembly checkpoint  regulation of mitotic cell cycle  microtubule binding  cell proliferation  positive regulation of peptidyl-threonine phosphorylation  anaphase-promoting complex binding  microtubule cytoskeleton  kinase activity  protein ubiquitination  peptidyl-serine phosphorylation  protein kinase binding  regulation of mitotic metaphase/anaphase transition  midbody  anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process  G2 DNA damage checkpoint  protein destabilization  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  polar body extrusion after meiotic divisions  negative regulation of apoptotic process  regulation of protein binding  establishment of protein localization  negative regulation of cyclin-dependent protein serine/threonine kinase activity  positive regulation of proteolysis  response to antibiotic  spindle midzone  centrosome organization  positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle  regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle  positive regulation of ubiquitin-protein transferase activity  regulation of cell cycle  protein localization to chromatin  
    Pathways : BIOCARTACell Cycle: G2/M Checkpoint [Genes]   
    Pathways : KEGGFoxO signaling pathway    Cell cycle    Oocyte meiosis    Progesterone-mediated oocyte maturation   
    REACTOMEP53350 [protein]
    REACTOME PathwaysREACT_115566 Cell Cycle [pathway]
    REACTOME PathwaysREACT_21300 Mitotic M-M/G1 phases [pathway]
    Protein Interaction DatabasePLK1
    Wikipedia pathwaysPLK1
    Gene fusion - rearrangments
    Polymorphisms : SNP, mutations, diseases
    SNP Single Nucleotide Polymorphism (NCBI)PLK1
    SNP (GeneSNP Utah)PLK1
    SNP : HGBasePLK1
    Genetic variants : HAPMAPPLK1
    1000_GenomesPLK1 
    ICGC programENSG00000166851 
    CONAN: Copy Number AnalysisPLK1 
    Somatic Mutations in Cancer : COSMICPLK1 
    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
    DECIPHER (Syndromes)16:23690201-23701688
    Mutations and Diseases : HGMDPLK1
    OMIM602098   
    MedgenPLK1
    GENETestsPLK1
    Disease Genetic AssociationPLK1
    Huge Navigator PLK1 [HugePedia]  PLK1 [HugeCancerGEM]
    Genomic VariantsPLK1  PLK1 [DGVbeta]
    Exome VariantPLK1
    dbVarPLK1
    ClinVarPLK1
    snp3D : Map Gene to Disease5347
    DGIdb (Curated mutations)PLK1
    DGIdb (Drug Gene Interaction db)PLK1
    General knowledge
    Homologs : HomoloGenePLK1
    Homology/Alignments : Family Browser (UCSC)PLK1
    Phylogenetic Trees/Animal Genes : TreeFamPLK1
    Chemical/Protein Interactions : CTD5347
    Chemical/Pharm GKB GenePA33410
    Clinical trialPLK1
    Cancer Resource (Charite)ENSG00000166851
    Other databases
    Probes
    Litterature
    PubMed424 Pubmed reference(s) in Entrez
    CoreMinePLK1
    GoPubMedPLK1
    iHOPPLK1

    Bibliography

    Cell cycle- and terminal differentiation-associated regulation of the mouse mRNA encoding a conserved mitotic protein kinase.
    Lake RJ, Jelinek WR
    Molecular and cellular biology. 1993 ; 13 (12) : 7793-7801.
    PMID 7902533
     
    Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5.
    Golsteyn RM, Schultz SJ, Bartek J, Ziemiecki A, Ried T, Nigg EA
    Journal of cell science. 1994 ; 107 ( Pt 6) : 1509-1517.
    PMID 7962193
     
    Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase.
    Hamanaka R, Maloid S, Smith MR, O'Connell CD, Longo DL, Ferris DK
    Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research. 1994 ; 5 (3) : 249-257.
    PMID 8018557
     
    Plk is an M-phase-specific protein kinase and interacts with a kinesin-like protein, CHO1/MKLP-1.
    Lee KS, Yuan YL, Kuriyama R, Erikson RL
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    PMID 8524282
     
    Antibody microinjection reveals an essential role for human polo-like kinase 1 (Plk1) in the functional maturation of mitotic centrosomes.
    Lane HA, Nigg EA
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    The mouse Plk gene: structural characterization, chromosomal localization and identification of a processed Plk pseudogene.
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    Neuronal polo-like kinase in Alzheimer disease indicates cell cycle changes.
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    Expression of polo-like kinase (PLK1) in thin melanomas: a novel marker of metastatic disease.
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    Journal of cutaneous pathology. 2002 ; 29 (6) : 354-358.
    PMID 12135466
     
    Role of Polo-like kinase CDC5 in programming meiosis I chromosome segregation.
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    PMID 12663816
     
    M phase-specific phosphorylation of BRCA2 by Polo-like kinase 1 correlates with the dissociation of the BRCA2-P/CAF complex.
    Lin HR, Ting NS, Qin J, Lee WH
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    PMID 12815053
     
    Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells.
    Liu X, Erikson RL
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    PMID 12732729
     
    Polo-like kinase 1 (PLK1) is overexpressed in primary colorectal cancers.
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    Cancer science. 2003 ; 94 (2) : 148-152.
    PMID 12708489
     
    Polo-like kinase 1 and Chk2 interact and co-localize to centrosomes and the midbody.
    Tsvetkov L, Xu X, Li J, Stern DF
    The Journal of biological chemistry. 2003 ; 278 (10) : 8468-8475.
    PMID 12493754
     
    Polo-like kinase 1 (Plk1) inhibits p53 function by physical interaction and phosphorylation.
    Ando K, Ozaki T, Yamamoto H, Furuya K, Hosoda M, Hayashi S, Fukuzawa M, Nakagawara A
    The Journal of biological chemistry. 2004 ; 279 (24) : 25549-25561.
    PMID 15024021
     
    Hierarchical requirement of SWI/SNF in retinoblastoma tumor suppressor-mediated repression of Plk1.
    Gunawardena RW, Siddiqui H, Solomon DA, Mayhew CN, Held J, Angus SP, Knudsen ES
    The Journal of biological chemistry. 2004 ; 279 (28) : 29278-29285.
    PMID 15105433
     
    Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC Inhibitor Emi1.
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    Molecular biology of the cell. 2004 ; 15 (12) : 5623-5634.
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    Phosphorylation of BRCA2 by the Polo-like kinase Plk1 is regulated by DNA damage and mitotic progression.
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    PMID 14647413
     
    Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells.
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    Molecular interactions of Polo-like-kinase 1 with the mitotic kinesin-like protein CHO1/MKLP-1.
    Liu X, Zhou T, Kuriyama R, Erikson RL
    Journal of cell science. 2004 ; 117 (Pt 15) : 3233-3246.
    PMID 15199097
     
    Polo-like kinase isoform expression is a prognostic factor in ovarian carcinoma.
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    British journal of cancer. 2004 ; 90 (4) : 815-821.
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    Polo-like kinase 1 is overexpressed in prostate cancer and linked to higher tumor grades.
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    The Prostate. 2004 ; 60 (3) : 240-245.
    PMID 15176053
     
    Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.
    Yamada S, Ohira M, Horie H, Ando K, Takayasu H, Suzuki Y, Sugano S, Hirata T, Goto T, Matsunaga T, Hiyama E, Hayashi Y, Ando H, Suita S, Kaneko M, Sasaki F, Hashizume K, Ohnuma N, Nakagawara A
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    Polo-like kinases and oncogenesis.
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    PMID 15640842
     
    Expression of Polo-Like Kinase (PLK1) in non-Hodgkin's lymphomas.
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    Polo-like kinases (Plks) and cancer.
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    Differential regulation of polo-like kinase 1, 2, 3, and 4 gene expression in mammalian cells and tissues.
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    PMID 15640841
     
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    Contributor(s)

    Written04-2005Ayse Elif Erson, Elizabeth M. Petty

    Citation

    This paper should be referenced as such :
    Erson, AE ; Petty, EM
    PLK1 (polo-like kinase 1 (Drosophila))
    Atlas Genet Cytogenet Oncol Haematol. 2005;9(3):219-221.
    Free online version   Free pdf version   [Bibliographic record ]
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