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Article Dans Une Revue Journal of Cell Biology Année : 2010

Subgroup II PAK-mediated phosphorylation regulates Ran activity during mitosis.

Résumé

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-bound 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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hal-00533751 , version 1 (28-05-2021)

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Paternité - Pas d'utilisation commerciale - Partage selon les Conditions Initiales

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Guillaume Bompard, Gabriel Rabeharivelo, Marie Frank, Julien Cau, Claude Delsert, et al.. Subgroup II PAK-mediated phosphorylation regulates Ran activity during mitosis.. Journal of Cell Biology, 2010, 190 (5), pp.807-22. ⟨10.1083/jcb.200912056⟩. ⟨hal-00533751⟩
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