Skip to Main content Skip to Navigation
Journal articles

Maternal embryonic leucine zipper kinase is stabilized in mitosis by phosphorylation and is partially degraded upon mitotic exit.

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.
Complete list of metadatas

https://www.hal.inserm.fr/inserm-00480065
Contributor : Hervé de Villemeur <>
Submitted on : Monday, May 3, 2010 - 2:33:27 PM
Last modification on : Wednesday, May 16, 2018 - 11:22:33 AM

Identifiers

Citation

Caroline Badouel, Isabelle Chartrain, Joëlle Blot, Jean-Pierre Tassan. Maternal embryonic leucine zipper kinase is stabilized in mitosis by phosphorylation and is partially degraded upon mitotic exit.. Experimental Cell Research, Elsevier, 2010, 316 (13), pp.2166-73. ⟨10.1016/j.yexcr.2010.04.019⟩. ⟨inserm-00480065⟩

Share

Metrics

Record views

229