Biology:MELK
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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 expression is elevated in a number of cancers and is an active research target for pharmacological inhibition.[5]
MELK was previously believed to be essential for cancer cell proliferation. However, recent research using CRISPR has demonstrated that MELK is fully dispensable for cancer cell growth, casting doubt on the rationale for targeting this protein in patients. The results are dependent on the experimental design. Therefore, there is a need for further research. [6][7][8][9]
Interactions
MELK has been shown to interact with CDC25B.[10]
References
- ↑ "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. February 1996. doi:10.1093/dnares/3.1.17. PMID 8724849.
- ↑ "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. June 1997. doi:10.1002/(SICI)1098-2795(199706)47:2<148::AID-MRD4>3.0.CO;2-M. PMID 9136115.
- ↑ "Entrez Gene: MELK maternal embryonic leucine zipper kinase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9833.
- ↑ "Expression of Melk, a new protein kinase, during early mouse development". Developmental Dynamics 215 (4): 344–51. August 1999. doi:10.1002/(SICI)1097-0177(199908)215:4<344::AID-AJA6>3.0.CO;2-H. PMID 10417823.
- ↑ "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. November 2005. doi:10.1158/0008-5472.CAN-04-4531. PMID 16266996.
- ↑ "CRISPR/Cas9 mutagenesis invalidates a putative cancer dependency targeted in on-going clinical trials". eLife 6. March 2017. doi:10.7554/eLife.24179. PMID 28337968.
- ↑ "MELK is not necessary for the proliferation of basal-like breast cancer cells". eLife 6. September 2017. doi:10.7554/eLife.26693. PMID 28926338.
- ↑ "MELK expression correlates with tumor mitotic activity but is not required for cancer growth". eLife 7. February 2018. doi:10.7554/eLife.32838. PMID 29417930.
- ↑ "Challenges in validating candidate therapeutic targets in cancer". eLife 7. February 2018. doi:10.7554/eLife.32402. PMID 29417929.
- ↑ "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation". Oncogene 21 (50): 7630–41. October 2002. doi:10.1038/sj.onc.1205870. PMID 12400006.
Further reading
- "Involvement of maternal embryonic leucine zipper kinase (MELK) in mammary carcinogenesis through interaction with Bcl-G, a pro-apoptotic member of the Bcl-2 family". Breast Cancer Research 9 (1): R17. 2007. doi:10.1186/bcr1650. PMID 17280616.
- "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. November 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- "Substrate specificity and activity regulation of protein kinase MELK". The Journal of Biological Chemistry 280 (48): 40003–11. December 2005. doi:10.1074/jbc.M507274200. PMID 16216881.
- "Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1". The Journal of Biological Chemistry 279 (10): 8642–7. March 2004. doi:10.1074/jbc.M311466200. PMID 14699119.
- "Human pEg3 kinase associates with and phosphorylates CDC25B phosphatase: a potential role for pEg3 in cell cycle regulation". Oncogene 21 (50): 7630–41. October 2002. doi:10.1038/sj.onc.1205870. PMID 12400006.
- "Phosphorylation of a novel zinc-finger-like protein, ZPR9, by murine protein serine/threonine kinase 38 (MPK38)". The Biochemical Journal 361 (Pt 3): 597–604. February 2002. doi:10.1042/0264-6021:3610597. PMID 11802789.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Cloning and expression of a cDNA encoding a novel protein serine/threonine kinase predominantly expressed in hematopoietic cells". Gene 195 (2): 295–301. August 1997. doi:10.1016/S0378-1119(97)00181-9. PMID 9305775.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
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