Data/hora: 10/06/2024 07:37:01

Provedor de dados: 	5	
País: 	France	
Título: 	Subgroup II PAK-mediated phosphorylation regulates Ran activity during mitosis	
Autores: 	Bompard, Guillaume; Rabeharivelo, Gabriel; Frank, Marie; Cau, Julien; Delsert, Claude; Morin, Nathalie.	
Data: 	2010-09	
Ano: 	2010	
Resumo: 	Ran is an essential GTPase that controls nucleocytoplasmic transport, mitosis, and nuclear envelope formation. These functions are regulated by interaction of Ran with different partners, and by formation of a Ran-GTP gradient emanating from chromatin. Here, we identify a novel level of Ran regulation. We show that Ran is a substrate for p21-activated kinase 4 (PAK4) and that its phosphorylation on serine-135 increases during mitosis. The endogenous phosphorylated Ran and active PAK4 dynamically associate with different components of the microtubule spindle during mitotic progression. A GDP-ound Ran phosphomimetic mutant cannot undergo RCC1-mediated GDP/GTP exchange and cannot induce microtubule asters in mitotic Xenopus egg extracts. Conversely, phosphorylation of GTP-bound Ran facilitates aster nucleation. Finally, phosphorylation of Ran on serine-135 impedes its binding to RCC1 and RanGAP1. Our study suggests that PAK4-mediated phosphorylation of GDP- or GTP-bound Ran regulates the assembly of Ran-dependent complexes on the mitotic spindle.	
Tipo: 	Text	
Idioma: 	Inglês	
Identificador: 	http://archimer.ifremer.fr/doc/00014/12502/9353.pdf

DOI:10.1083/jcb.200912056	
Editor: 	Rockefeller Univ Press	
Relação: 	http://archimer.ifremer.fr/doc/00014/12502/	
Formato: 	application/pdf	
Fonte: 	Journal Of Cell Biology (0021-9525) (Rockefeller Univ Press), 2010-09 , Vol. 190 , N. 5 , P. 807-822	
Fonte: 	2010 by The Rockefeller University Press