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Maternal Embryonic Leucine Zipper Kinase (MELK): a Novel Regulator in Cell Cycle Control, Embryonic Development, and Cancer

Overview
Journal Int J Mol Sci
Publisher MDPI
Date 2013 Nov 5
PMID 24185907
Citations 47
Authors
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Abstract

Maternal embryonic leucine zipper kinase (MELK) functions as a modulator of intracellular signaling and affects various cellular and biological processes, including cell cycle, cell proliferation, apoptosis, spliceosome assembly, gene expression, embryonic development, hematopoiesis, and oncogenesis. In these cellular processes, MELK functions by binding to numerous proteins. In general, the effects of multiple protein interactions with MELK are oncogenic in nature, and the overexpression of MELK in kinds of cancer provides some evidence that it may be involved in tumorigenic process. In this review, our current knowledge of MELK function and recent discoveries in MELK signaling pathway were discussed. The regulation of MELK in cancers and its potential as a therapeutic target were also described.

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References
1.
Gil M, Yang Y, Lee Y, Choi I, Ha H . Cloning and expression of a cDNA encoding a novel protein serine/threonine kinase predominantly expressed in hematopoietic cells. Gene. 1997; 195(2):295-301. DOI: 10.1016/s0378-1119(97)00181-9. View

2.
Kim A, Khursigara G, Sun X, Franke T, Chao M . Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1. Mol Cell Biol. 2001; 21(3):893-901. PMC: 86680. DOI: 10.1128/MCB.21.3.893-901.2001. View

3.
Badouel C, Korner R, Frank-Vaillant M, Couturier A, Nigg E, Tassan J . M-phase MELK activity is regulated by MPF and MAPK. Cell Cycle. 2006; 5(8):883-9. DOI: 10.4161/cc.5.8.2683. View

4.
Ku J, Shin Y, Kim D, Kim K, Choi J, Hong S . Establishment and characterization of 13 human colorectal carcinoma cell lines: mutations of genes and expressions of drug-sensitivity genes and cancer stem cell markers. Carcinogenesis. 2010; 31(6):1003-9. DOI: 10.1093/carcin/bgq043. View

5.
Niesler C, Myburgh K, Moore F . The changing AMPK expression profile in differentiating mouse skeletal muscle myoblast cells helps confer increasing resistance to apoptosis. Exp Physiol. 2006; 92(1):207-17. DOI: 10.1113/expphysiol.2006.034736. View