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Vol. 12, Issue 2, 437-448, February 2001
and
*Institut Curie, Section Recherche, Unité Mixte de Recherche
144 Centre National de la Recherche Scientifique, 75248 Paris Cedex 05, France; and Stathmin/Op 18 is a microtubule (MT) dynamics-regulating protein
that has been shown to have both catastrophe-promoting and tubulin-sequestering activities. The level of stathmin/Op18
phosphorylation was proved both in vitro and in vivo to be important in
modulating its MT-destabilizing activity. To understand the in vivo
regulation of stathmin/Op18 activity, we investigated whether MT
assembly itself could control phosphorylation of stathmin/Op18 and thus its MT-destabilizing activity. We found that MT nucleation by centrosomes from Xenopus sperm or somatic cells and MT
assembly promoted by dimethyl sulfoxide or paclitaxel induced
stathmin/Op18 hyperphosphorylation in Xenopus egg
extracts, leading to new stathmin/Op18 isoforms phosphorylated on Ser
16. The MT-dependent phosphorylation of stathmin/Op18 took place in
interphase extracts as well, and was also observed in somatic cells. We
show that the MT-dependent phosphorylation of stathmin/Op18 on Ser 16 is mediated by an activity associated to the MTs, and that it is
responsible for the stathmin/Op18 hyperphosphorylation reported to be
induced by the addition of "mitotic chromatin." Our results suggest
the existence of a positive feedback loop, which could represent a
novel mechanism contributing to MT network control.
Institut National de la Santé et de la
Recherche Médicale U440, Institut du Fer à Moulin, F-75005
Paris, France
Present address: Institut Curie, Section
Recherche, UMR 144 CNRS, 26 rue d'Ulm, 75248 Paris Cedex 05, France.
§
Corresponding author: E-mail address:
mbornens{at}curie.fr.
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