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J Biol Chem, Vol. 274, Issue 44, 31719-31726, October 29, 1999
From the Molecular Oncology Group, Stimulation of the hepatocyte growth factor
receptor tyrosine kinase, Met, induces the inherent morphogenic program
of epithelial cells. The multisubstrate binding protein Gab1
(Grb2-associated binder-1) is the
major phosphorylated protein in epithelial cells following activation
of Met. Gab1 contains a pleckstrin homology domain and multiple
tyrosine residues that act to couple Met with multiple signaling
proteins. Met receptor mutants that are impaired in their association
with Gab1 fail to induce a morphogenic program in epithelial cells,
which is rescued by overexpression of Gab1. The Gab1 pleckstrin
homology domain binds to phosphatidylinositol 3,4,5-trisphosphate and
contains conserved residues, shown from studies of other pleckstrin
homology domains to be crucial for phospholipid binding. Mutation
of conserved phospholipid binding residues tryptophan 26 and arginine
29, generates Gab1 proteins with decreased phosphatidylinositol
3,4,5-trisphosphate binding, decreased localization at sites of
cell-cell contact, and reduced ability to rescue
Met-dependent morphogenesis. We conclude that the ability
of the Gab1 pleckstrin homology domain to bind phosphatidylinositol 3,4,5-trisphosphate is critical for subcellular localization of Gab1
and for efficient morphogenesis downstream from the Met receptor.
A Conserved Inositol Phospholipid Binding Site within the
Pleckstrin Homology Domain of the Gab1 Docking Protein Is Required for
Epithelial Morphogenesis
,,
**
Medicine, Oncology, and
** Biochemistry, McGill University, Montréal, Québec, Canada
H31 1A1 and the Departments of § Microbiology and Immunology
and ¶ Pharmacology, Kimmel Cancer Institute,
Philadelphia, Pennsylvania 19107
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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