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J Biol Chem, Vol. 275, Issue 18, 13842-13848, May 5, 2000
From the Grb2-associated binder-1 (Gab1) is a multisite
docking protein containing a pleckstrin homology (PH) domain, multiple
potential tyrosine phosphorylation sites, and several proline-rich
sequences. Gab1 becomes tyrosine-phosphorylated in cells stimulated
with growth factors, cytokines, and ligands for G protein-coupled
receptors. A major Gab1-binding protein detected in cells treated with
extracellular stimuli is the tyrosine phosphatase, SHP2. Although the
role of SHP2-Gab1 interaction in cell signaling has not yet been
characterized, SHP2 is known to mediate mitogen-activated protein (MAP)
kinase activation induced by the epidermal growth factor (EGF).
However, the mechanism by which the SHP2 phosphatase exerts a positive signaling role remains obscure. In this study, we prepared Gab1 mutants
lacking the SHP2 binding site (Gab1Y627F), the phosphatidylinositol 3-kinase (PI3K) binding sites (Gab1
Requirement of SHP2 Binding to Grb2-associated Binder-1 for
Mitogen-activated Protein Kinase Activation in Response to
Lysophosphatidic Acid and Epidermal Growth Factor*
§,§,¶,
, and§¶**
Molecular Oncology Program, H. Lee Moffitt
Cancer Center and Research Institute, Tampa, Florida 33612, the
Departments of § Medical Microbiology and Immunology, and
¶ Biochemistry and Molecular Biology, University of South Florida,
Tampa, Florida 33612, and the Department of Neurobiology,
University of Alabama, Birmingham, Alabama 35294
PI3K), and the PH domain
(Gab1PH). Expression of Gab1Y627F blocked the extracellular
signal-regulated kinase-2 (ERK2) activation by lysophosphatidic acid
(LPA) and EGF. Conversely, expression of the wild-type Gab1 in HEK293
cells augmented the LPA receptor Edg2-mediated ERK2 activation. Whereas the PH domain was required for Gab1 mediation of ERK2 activation by
LPA, it was not essential for EGF-induced ERK2 activation. Expression
of Gab1PI3K had no apparent effect on ERK2 activation by LPA and EGF
in the cells that we have examined. These results establish a role for
Gab1 in the LPA-induced MAP kinase pathway and clearly demonstrate that
Gab1-SHP2 interaction is essential for ERK2 activation by LPA and EGF.
These findings also suggest that the positive role of SHP2 in the MAP
kinase pathway depends on its interaction with Gab1.
*
This work was supported in part by Junior Faculty Research
Award JFRA-647 from the American Cancer Society, National Institutes of
Health Grant CA77467, American Heart Association Florida Affiliate Grant 9810152FL (to J. W.), National Institutes of Health Grants NS34062 and NS39401 (to L. M.), and National Institutes of Health Training Grant T32 DA 07245 (to J. M. C.).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.
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