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PMID: 11179426 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Stathmin/Op18 phosphorylation is regulated by microtubule assembly.

Molecular biology of the cell ·Vol. 12 ·No. 2 ·2001-02-00 ·Pages 437-48

Küntziger T, Gavet O, Manceau V, Sobel A, Bornens M

Abstract

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.

MeSH Terms
Animals Cell Nucleus/drug effects,metabolism Centrosome/metabolism Enzyme Inhibitors/pharmacology Female HeLa Cells Humans Interphase/physiology Male Microtubule Proteins Microtubules/drug effects,metabolism Nocodazole/pharmacology Ovum/metabolism,ultrastructure Paclitaxel/pharmacology Phosphoproteins/metabolism Phosphorylation Protein Isoforms Serine/metabolism Spermatozoa/metabolism,ultrastructure Stathmin Xenopus Xenopus Proteins
Chemicals
Enzyme Inhibitors Microtubule Proteins Phosphoproteins Protein Isoforms STMN1 protein, Xenopus STMN1 protein, human Stathmin Xenopus Proteins Serine Paclitaxel Nocodazole
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Küntziger T
Institut Curie, Section Recherche, Unité Mixte de Recherche 144 Centre National de la Recherche Scientifique, 75248 Paris Cedex 05, France.
Gavet O
Manceau V
Sobel A
Bornens M
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
Published
2001-02-00
Pages
437-48
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC30954
Subset
IM
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