The Gab1 PH Domain Is Required for Localization of Gab1 at Sites of Cell-Cell Contact and Epithelial Morphogenesis Downstream from the Met Receptor Tyrosine Kinase

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Molecular and Cellular Biology, March 1999, p. 1784-1799, Vol. 19, No. 3
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Gab1 PH Domain Is Required for Localization of Gab1 at Sites of Cell-Cell Contact and Epithelial Morphogenesis Downstream from the Met Receptor Tyrosine Kinase

Christiane R. Maroun,¹ Marina Holgado-Madruga,² Isabelle Royal,¹ Monica A. Naujokas,¹ Tanya M. Fournier,³ Albert J. Wong,²^,⁴ and Morag Park¹^,³^,⁵^,^*

Departments of Medicine,¹ Oncology,⁵ and Biochemistry,³ Molecular Oncology Group, Royal Victoria Hospital, McGill University, Montreal, Quebec, Canada H3A 1A1, and Departments of Microbiology and Immunology² and Pharmacology,⁴ Kimmel Cancer Institute, Philadelphia, Pennsylvania 19107

Received 10 August 1998/Returned for modification 23 September 1998/Accepted 30 November 1998

Stimulation of the hepatocyte growth factor (HGF) receptor tyrosine kinase, Met, induces mitogenesis, motility, invasion,and branching tubulogenesis of epithelial and endothelial celllines in culture. We have previously shown that Gab1 is the majorphosphorylated protein following stimulation of the Met receptorin epithelial cells that undergo a morphogenic program in responseto HGF. Gab1 is a member of the family of IRS-1-like multisubstratedocking proteins and, like IRS-1, contains an amino-terminal pleckstrinhomology domain, in addition to multiple tyrosine residues thatare potential binding sites for proteins that contain SH2 or PTBdomains. Following stimulation of epithelial cells with HGF, Gab1associates with phosphatidylinositol 3-kinase and the tyrosinephosphatase SHP2. Met receptor mutants that are impaired in theirassociation with Gab1 fail to induce branching tubulogenesis.Overexpression of Gab1 rescues the Met-dependent tubulogenic responsein these cell lines. The ability of Gab1 to promote tubulogenesisis dependent on its pleckstrin homology domain. Whereas the wild-typeGab1 protein is localized to areas of cell-cell contact, a Gab1protein lacking the pleckstrin homology domain is localized predominantlyin the cytoplasm. Localization of Gab1 to areas of cell-cell contactis inhibited by LY294002, demonstrating that phosphatidylinositol3-kinase activity is required. These data show that Gab1 is animportant mediator of branching tubulogenesis downstream fromthe Met receptor and identify phosphatidylinositol 3-kinase andthe Gab1 pleckstrin homology domain as crucial for subcellularlocalization of Gab1 and biologicalresponses.

^* Corresponding author. Mailing address: Molecular Oncology Group, Royal Victoria Hospital, 687 Pine Ave. West, Rm H5.10, Montreal,Quebec, Canada H3A 1A1. Phone: (514) 842-1231 ext. 5845. Fax:(514) 843-1478. E-mail: morag{at}lan1.molonc.mcgill.ca.

Molecular and Cellular Biology, March 1999, p. 1784-1799, Vol. 19, No. 3
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

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