| Registro completo |
| Provedor de dados: |
ArchiMer
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| País: |
France
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| Título: |
Subgroup II PAK-mediated phosphorylation regulates Ran activity during mitosis
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| Autores: |
Bompard, Guillaume
Rabeharivelo, Gabriel
Frank, Marie
Cau, Julien
Delsert, Claude
Morin, Nathalie
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| Data: |
2010-09
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| Ano: |
2010
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| 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.
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| Tipo: |
Text
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| Idioma: |
Inglês
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| Identificador: |
http://archimer.ifremer.fr/doc/00014/12502/9353.pdf
DOI:10.1083/jcb.200912056
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| Editor: |
Rockefeller Univ Press
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| Relação: |
http://archimer.ifremer.fr/doc/00014/12502/
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| Formato: |
application/pdf
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| Fonte: |
Journal Of Cell Biology (0021-9525) (Rockefeller Univ Press), 2010-09 , Vol. 190 , N. 5 , P. 807-822
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| Direitos: |
2010 by The Rockefeller University Press
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