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Vol. 11, Issue 5, 1709-1725, May 2000
¶**
*Molecular Oncology Group, McGill University Hospital Center, and
Departments of Hepatocyte growth factor (HGF), the ligand for the Met receptor
tyrosine kinase, is a potent modulator of epithelial-mesenchymal transition and dispersal of epithelial cells, processes that play crucial roles in tumor development, invasion, and metastasis. Little is
known about the Met-dependent proximal signals that regulate these
events. We show that HGF stimulation of epithelial cells leads to
activation of the Rho GTPases, Cdc42 and Rac, concomitant with the
formation of filopodia and lamellipodia. Notably, HGF-dependent activation of Rac but not Cdc42 is dependent on
phosphatidylinositol 3-kinase. Moreover, HGF-induced
lamellipodia formation and cell spreading require
phosphatidylinositol 3-kinase and are inhibited by dominant
negative Cdc42 or Rac. HGF induces activation of the Cdc42/Rac-regulated p21-activated kinase (PAK) and c-Jun N-terminal kinase, and translocation of Rac, PAK, and Rho-dependent Rho-kinase to
membrane ruffles. Use of dominant negative and activated mutants reveals an essential role for PAK but not Rho-kinase in HGF-induced epithelial cell spreading, whereas Rho-kinase activity is required for
the formation of focal adhesions and stress fibers in response to HGF.
We conclude that PAK and Rho-kinase play opposing roles in
epithelial-mesenchymal transition induced by HGF, and provide new
insight regarding the role of Cdc42 in these events.
Anatomy and Cell Biology,
Biochemistry, Medicine, and
¶Oncology, McGill University, Montreal, Quebec, Canada,
H3A 1A1; and §Division of Signal Transduction, Nara
Institute of Science and Technology, Ikoma 630-0101, Japan
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