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Papers In Press, published online ahead of print October 31, 2000
J. Biol. Chem, 10.1074/jbc.C000635200
Submitted on September 12, 2000
Revised on October 27, 2000
Accepted on October 31, 2000
MRC Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT
Corresponding Author: alan.hall{at}ucl.ac.uk
Using two-dimensional gel electrophoresis coupled to matrix-assisted laser desorption/ionization mass spectrometry in combination with post-source decay analysis, we have identified a rapid protein phosphorylation event at residue serine 16 of stathmin 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. Since stathmin destabilizes microtubules and this is inhibited by phosphorylation at residue 16, Rac and Cdc42 can potentially regulate both F-actin and microtubule dynamics.
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