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J. Biol. Chem., Vol. 276, Issue 3, 1677-1680, January 19, 2001
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§,
,§§
From the We have identified a rapid protein
phosphorylation event at residue serine 16 of stathmin using
two-dimensional gel electrophoresis coupled to matrix-assisted laser
desorption/ionization mass spectrometry in combination with post-source
decay analysis, which is induced by the epidermal growth factor
receptor. Phosphorylation is specifically mediated by the small
GTPases Rac and Cdc42 and their common downstream target, the
serine/threonine kinase p65PAK. Both GTPases have previously
been shown to regulate the dynamics of actin polymerization. Because
stathmin destabilizes microtubules, and this process is inhibited by
phosphorylation at residue 16, Rac and Cdc42 can potentially regulate
both F-actin and microtubule dynamics.
Medical Research Council Laboratory
for Molecular Cell Biology, Cancer Research Campaign Oncogene
and Signal Transduction Group, and the
Department of Biochemistry, University
College London, Gower Street, London WC1E 6BT, United Kingdom, the
¶ Department of Biochemistry and Medical Protein Research,
Flanders Interuniversity Institute for Biotechnology, Ghent University,
B-900 Belgium, and ** INSERM U440, IFM, 17 rue du Fer
à Moulin, 75005 Paris, France
Postdoctoral Fellow of the Fund for Scientific Research,
Flanders, Belgium (F. W. O.-Vlaanderen).
§§
To whom correspondence should be addressed. E-mail:
alan. hall@ucl.ac.uk.
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