Nek9 is a Plk1-activated kinase that controls early centrosome separation through Nek6/7 and Eg5-Reference-Cited by-同舟云学术

Nek9 is a Plk1-activated kinase that controls early centrosome separation through Nek6/7 and Eg5

Published:2011-06-03 Issue:13 Volume:30 Page:2634-2647
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:

Author:

Bertran M Teresa¹,Sdelci Sara¹,Regué Laura¹,Avruch Joseph²,Caelles Carme¹³,Roig Joan¹

Affiliation:

1. Cell Signalling Research Group, Molecular Medicine Program, Institute for Research in Biomedicine (IRB Barcelona); Barcelona Spain

2. Department of Molecular Biology and Medical Services, Massachusetts General Hospital and Department of Medicine, Harvard Medical School; Boston MA USA

3. Department of Biochemistry and Molecular Biology (Pharmacy), Universitat de Barcelona; Barcelona Spain

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference42 articles.

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3. Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150;Blangy;J Biol Chem,1997

4. Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo;Blangy;Cell,1995

5. Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates;Elia;Science,2003

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