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Volume 272, Number 52, Issue of December 26, 1997 pp. 33105-33110
(Received for publication, September 9, 1997, and in revised form, October 20, 1997)
,
,
From the The Rho family of GTPases plays an important role
in the control of cell shape, adhesion, movement, and growth. Several
guanine nucleotide exchange factors have been identified that activate Rho family GTPases by promoting the binding of GTP to these proteins. However, little is known concerning the regulation of these GDP/GTP exchange factors. In this study, we demonstrate that lysophosphatidic acid (LPA) induces a rapid, sustainable phosphorylation of the Rac1-specific nucleotide exchange factor Tiam1 in Swiss 3T3
fibroblasts. LPA stimulated Tiam1 phosphorylation in a
dose-dependent manner, and the protein was phosphorylated
on threonine, but not tyrosine or serine. Tiam1 phosphorylation was
also induced by platelet-derived growth factor, endothelin-1, bombesin,
and bradykinin but not by epidermal growth factor. Significantly,
pretreatment of Swiss 3T3 fibroblasts with 1 µM
phorbol 12-myristate 13-acetate for 24 h, or with the selective
protein kinase C inhibitor Ro-31-8220, reduced LPA-stimulated
phosphorylation of Tiam1 by approximately 75%. Moreover, acute
stimulation with 100 nM phorbol 12-myristate 13-acetate was
sufficient to induce Tiam1 phosphorylation in vivo, and
protein kinase C could phosphorylate purified Tiam1 on threonine residues in vitro. These data indicate that agonist-induced
phosphorylation of Tiam1 is a general mechanism and suggest that it is
likely to be important in its regulation. Protein kinase C appears to play a key role in phosphorylation of Tiam1.
Howard Hughes Medical Institute and
Department of Molecular Physiology and Biophysics, Vanderbilt
University School of Medicine, Nashville, Tennessee 37232-0295 and the
§ Division of Cell Biology, The Netherlands Cancer
Institute, Amsterdam, The Netherlands
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