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• W2022982388 startingPage "2166" @default.
• W2022982388 abstract "MELK (maternal embryonic leucine zipper kinase) is a cell cycle dependent protein kinase involved in diverse cell processes including cell proliferation, apoptosis, cell cycle and mRNA processing. Noticeably, MELK expression is increased in cancerous tissues, upon cell transformation and in mitotically-blocked cells. The question of how MELK protein level is controlled is therefore important. Here, we show that MELK protein is restricted to proliferating cells derived from either cancer or normal tissues and that MELK protein level is severely decreased concomitantly with other cell cycle proteins in cells which exit the cell cycle. Moreover, we demonstrate in human HeLa cells and Xenopus embryos that approximately half of MELK protein is degraded upon mitotic exit whereas another half remains stable during interphase. We show that the stability of MELK protein in M-phase is dependent on its phosphorylation state." @default.
• W2022982388 created "2016-06-24" @default.
• W2022982388 creator A5019650373 @default.
• W2022982388 creator A5056729136 @default.
• W2022982388 creator A5060054107 @default.
• W2022982388 creator A5091675402 @default.
• W2022982388 date "2010-08-01" @default.
• W2022982388 modified "2023-10-18" @default.
• W2022982388 title "Maternal embryonic leucine zipper kinase is stabilized in mitosis by phosphorylation and is partially degraded upon mitotic exit" @default.
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• W2022982388 doi "https://doi.org/10.1016/j.yexcr.2010.04.019" @default.
• W2022982388 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20420823" @default.
• W2022982388 hasPublicationYear "2010" @default.
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