@article {957076,
	title = {Mitotic MELK-eIF4B signaling controls protein synthesis and tumor cell survival},
	journal = {Proc Natl Acad Sci U S A},
	volume = {113},
	number = {35},
	year = {2016},
	month = {2016 Aug 30},
	pages = {9810-5},
	abstract = {The protein kinase maternal and embryonic leucine zipper kinase (MELK) is critical for mitotic progression of cancer cells; however, its mechanisms of action remain largely unknown. By combined approaches of immunoprecipitation/mass spectrometry and peptide library profiling, we identified the eukaryotic translation initiation factor 4B (eIF4B) as a MELK-interacting protein during mitosis and a bona fide substrate of MELK. MELK phosphorylates eIF4B at Ser406, a modification found to be most robust in the mitotic phase of the cell cycle. We further show that the MELK-eIF4B signaling axis regulates protein synthesis during mitosis. Specifically, synthesis of myeloid cell leukemia 1 (MCL1), an antiapoptotic protein known to play a role in cancer cell survival during cell division, depends on the function of MELK-elF4B. Inactivation of MELK or eIF4B results in reduced protein synthesis of MCL1, which, in turn, induces apoptotic cell death of cancer cells. Our study thus defines a MELK-eIF4B signaling axis that regulates protein synthesis during mitosis, and consequently influences cancer cell survival.},
	issn = {1091-6490},
	doi = {10.1073/pnas.1606862113},
	author = {Wang, Yubao and Begley, Michael and Li, Qing and Huang, Hai-Tsang and Lako, Ana and Eck, Michael J and Gray, Nathanael S and Mitchison, Timothy J. and Cantley, Lewis C and Zhao, Jean J}
}
