MELK

Revision as of 17:02, 27 November 2017 by en>Boghog (consistent citation formatting)
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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
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RefSeq (mRNA)

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RefSeq (protein)

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Maternal embryonic leucine zipper kinase (MELK) is an enzyme that in humans is encoded by the MELK gene.[1][2][3] MELK is a serine/threonine kinase belonging to the family of AMPK/snf1 protein kinases. MELK was first identified present as maternal mRNA in mouse embryos.[4] MELK has been shown to involved in progression through the cell cycle, possibly linked to its interaction with CDC25B.[5] MELK expression is elevated in a number of cancers and is an active research target for pharmacological inhibition.[6]

Interactions

MELK has been shown to interact with CDC25B.[7]

References

  1. Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N (February 1996). "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research. 3 (1): 17–24. doi:10.1093/dnares/3.1.17. PMID 8724849.
  2. Heyer BS, Warsowe J, Solter D, Knowles BB, Ackerman SL (June 1997). "New member of the Snf1/AMPK kinase family, Melk, is expressed in the mouse egg and preimplantation embryo". Molecular Reproduction and Development. 47 (2): 148–56. doi:10.1002/(SICI)1098-2795(199706)47:2<148::AID-MRD4>3.0.CO;2-M. PMID 9136115.
  3. "Entrez Gene: MELK maternal embryonic leucine zipper kinase".
  4. Heyer BS, Kochanowski H, Solter D (August 1999). "Expression of Melk, a new protein kinase, during early mouse development". Developmental Dynamics. 215 (4): 344–51. doi:10.1002/(SICI)1097-0177(199908)215:43.0.CO;2-H. PMID 10417823.
  5. Nakano I, Paucar AA, Bajpai R, Dougherty JD, Zewail A, Kelly TK, Kim KJ, Ou J, Groszer M, Imura T, Freije WA, Nelson SF, Sofroniew MV, Wu H, Liu X, Terskikh AV, Geschwind DH, Kornblum HI (August 2005). "Maternal embryonic leucine zipper kinase (MELK) regulates multipotent neural progenitor proliferation". The Journal of Cell Biology. 170 (3): 413–27. doi:10.1083/jcb.200412115. PMC 2171475. PMID 16061694.
  6. Gray D, Jubb AM, Hogue D, Dowd P, Kljavin N, Yi S, Bai W, Frantz G, Zhang Z, Koeppen H, de Sauvage FJ, Davis DP (November 2005). "Maternal embryonic leucine zipper kinase/murine protein serine-threonine kinase 38 is a promising therapeutic target for multiple cancers". Cancer Research. 65 (21): 9751–61. doi:10.1158/0008-5472.CAN-04-4531. PMID 16266996.
  7. Davezac N, Baldin V, Blot J, Ducommun B, Tassan JP (October 2002). "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation". Oncogene. 21 (50): 7630–41. doi:10.1038/sj.onc.1205870. PMID 12400006.

Further reading