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Vol. 11, Issue 8, 2565-2575, August 2000
and
*Department of Molecular Biology and Biochemistry, Osaka University
Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Japan; and Hepatocyte growth factor/scatter factor (HGF/SF) induces cell
scattering through the tyrosine kinase-type HGF/SF receptor c-Met. We
have previously shown that Rho small G protein (Rho) is involved in the
HGF/SF-induced scattering of Madin-Darby canine kidney (MDCK) cells by
regulating at least the assembly and disassembly of stress fibers and
focal adhesions, but it remains unknown how c-Met regulates Rho
activity. We have found here a novel signaling pathway of c-Met
consisting of SHP-2-Rho that regulates the assembly and disassembly of
stress fibers and focal adhesions in MDCK cells. SHP-2 is a
protein-tyrosine phosphatase that contains src homology-2 domains.
Expression of a dominant negative mutant of SHP-2 (SHP-2-C/S) markedly
increased the formation of stress fibers and focal adhesions in MDCK
cells and inhibited their scattering. C3, a Clostridium botulinum ADP-ribosyltransferase, and Y-27632, a specific
inhibitor for ROCK, reversed the stimulatory effect of SHP-2-C/S on
stress fiber formation and the inhibitory effect on cell scattering. Vav2 is a GDP/GTP exchange protein for Rho. Expression of a dominant negative mutant of Vav2 blocked the stimulatory effect of SHP-2-C/S on
stress fiber formation. Conversely, expression of mutants of Vav2 that
increased stress fiber formation inhibited HGF/SF-induced cell
scattering. These results indicate that SHP-2 physiologically modulates
the activity of Rho to form stress fibers and focal adhesions and
thereby regulates HGF/SF-induced cell scattering. In addition, Vav2 may
be involved in the SHP-2-Rho pathway.
Department of Dermatology, Kobe University
School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan
Corresponding author. E-mail
address: ytakai{at}molbio.med.osaka-u.ac.jp.
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