Data/hora: 02/06/2024 12:34:02

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