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J. Biol. Chem., Vol. 277, Issue 25, 22718-22724, June 21, 2002
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From the Dynamique du Cytosquelette, Laboratoire d'Enzymologie et
Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France
Stathmin is a phosphorylation-regulated
tubulin-binding protein. In vitro and in vivo
studies using nonphosphorylatable and pseudophosphorylated mutants of
stathmin have questioned the view that stathmin might act only as a
tubulin-sequestering factor. Stathmin was proposed to effectively
regulate microtubule dynamic instability by increasing the frequency of
catastrophe (the transition from steady growth to rapid
depolymerization), without interacting with tubulin. We have used a
noninvasive method to measure the equilibrium dissociation constants of
the T2S complexes of tubulin with stathmin,
pseudophosphorylated (4E)-stathmin, and diphosphostathmin. At both pH
6.8 and pH 7.4, the relative sequestering efficiency of the different
stathmin variants depends on the concentration of free tubulin,
i.e. on the dynamic state of microtubules. This control is
exerted in a narrow range of tubulin concentration due to the highly
cooperative binding of tubulin to stathmin. Changes in pH affect the
stability of tubulin-stathmin complexes but do not change stathmin
function. The 4E-stathmin mutant mimics inactive phosphorylated
stathmin at low tubulin concentration and sequesters tubulin almost as
efficiently as stathmin at higher tubulin concentration. We
propose that stathmin acts solely by sequestering tubulin,
without affecting microtubule dynamics, and that the effect of stathmin
phosphorylation on microtubule assembly depends on tubulin critical concentration.
The Effect of Stathmin Phosphorylation on Microtubule Assembly
Depends on Tubulin Critical Concentration*,
*
This work was supported in part by the Ligue Nationale
contre le Cancer.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains Fig. 1S.
To whom correspondence should be addressed: Dynamique du
Cytosquelette, Laboratoire d'Enzymologie et Biochimie Structurales, 1 Avenue de la Terrasse, CNRS, 91198 Gif-sur-Yvette, France. Tel.: 33-1-69-82-34-65; Fax: 33-1-69-82-31-29; E-mail:
carlier@lebs.cnrs-gif.fr.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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