FN Archimer Export Format
PT J
TI Subgroup II PAK-mediated phosphorylation regulates Ran activity during mitosis
BT 
AF BOMPARD, Guillaume
   RABEHARIVELO, Gabriel
   FRANK, Marie
   CAU, Julien
   DELSERT, Claude
   MORIN, Nathalie
AS 1:1,2,4;2:1,2,4;3:1,2,4;4:1,3,4;5:1,2,4,5;6:1,2,4;
FF 1:;2:;3:;4:;5:PDG-DOP-DCN-AGSAE-LGP;6:;
C1 Univ Montpellier 2, IFR 122, F-34293 Montpellier, France.
   CNRS, Ctr Rech Biochim Macromol, F-34293 Montpellier, France.
   CNRS, UPR 1142, Inst Human Genet, F-34396 Montpellier, France.
   Univ Montpellier 1, IFR 122, F-34293 Montpellier, France.
   IFREMER, Lab Genet & Pathol, F-17390 La Tremblade, France.
C2 UNIV MONTPELLIER, FRANCE
   CNRS, FRANCE
   CNRS, FRANCE
   UNIV MONTPELLIER, FRANCE
   IFREMER, FRANCE
SI MONTPELLIER
SE PDG-DOP-DCN-AGSAE-LGP
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 9.921
TC 34
UR https://archimer.ifremer.fr/doc/00014/12502/9353.pdf
LA English
DT Article
AB 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.
PY 2010
PD SEP
SO Journal Of Cell Biology
SN 0021-9525
PU Rockefeller Univ Press
VL 190
IS 5
UT 000281781300011
BP 807
EP 822
DI 10.1083/jcb.200912056
ID 12502
ER

EF