| Maternal embryonic leucine zipper kinase is stabilized in mitosis by phosphorylation and is partially degraded upon mitotic exit. | |
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MedLine Citation:
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PMID: 20420823 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Caroline Badouel; Isabelle Chartrain; Joëlle Blot; Jean-Pierre Tassan |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-04-24 |
Journal Detail:
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Title: Experimental cell research Volume: 316 ISSN: 1090-2422 ISO Abbreviation: Exp. Cell Res. Publication Date: 2010 Aug |
Date Detail:
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Created Date: 2010-07-08 Completed Date: 2010-07-29 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0373226 Medline TA: Exp Cell Res Country: United States |
Other Details:
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Languages: eng Pagination: 2166-73 Citation Subset: IM |
Copyright Information:
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Copyright 2010 Elsevier Inc. All rights reserved. |
Affiliation:
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CNRS UMR 6061 Génétique et Développement, Université de Rennes 1, IFR140 GFAS, Faculté de médecine, 2 avenue du Professeur Léon Bernard, CS 34317, 35043 Rennes Cedex, France. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Blotting, Western Cells, Cultured Embryo, Nonmammalian / cytology, enzymology* Endothelium, Vascular / cytology, enzymology* Fertilization Hela Cells Humans Male Mitosis / physiology* Phosphorylation Prostatic Neoplasms / enzymology*, pathology Protein-Serine-Threonine Kinases / metabolism* Umbilical Veins / cytology, enzymology Xenopus laevis / growth & development, metabolism |
| Chemical | |
Reg. No./Substance:
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EC 2.7.1.-/MELK protein, human; EC 2.7.11.1/Protein-Serine-Threonine Kinases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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