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J. Biol. Chem., Vol. 277, Issue 40, 36962-36969, October 4, 2002
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From the Medical Research Council Laboratory for Molecular Cell
Biology and the Department of Biochemistry and Molecular Biology,
University College London, Gower Street,
London WC1E 6BT, United Kingdom
Cadherins are transmembrane receptors that
mediate cell-cell adhesion. They play an essential role in
embryonic development and maintenance of tissue architecture. The Rho
family small GTPases regulate actin cytoskeletal dynamics in different
cell types. The function of two family members, Rho and Rac, is
required for the stability of cadherins at cell-cell contacts.
Consistent with the published data we have found that Rac is activated
upon induction of intercellular adhesion in epithelial cells. This
activation is dependent on functional cadherins (Nakagawa, M., Fukata,
M., Yamaga, M., Itoh, N., and Kaibuchi, K. (2001) J. Cell
Sci. 114, 1829-1838; Noren, N. K., Niessen, C. M.,
Gumbiner, B. M., and Burridge, K. (2001) J. Biol.
Chem. 276, 3305-3308). Here we show for the first time that
clustering of cadherins using antibody-coated beads is sufficient to
promote Rac activation. In the presence of Latrunculin B, Rac can be
partially activated by antibody-clustered cadherins. These results
suggest that actin polymerization is not required for initial Rac
activation. Contrary to what has been described before,
phosphatidylinositol 3-kinases are not involved in Rac activation
following cell-cell adhesion in keratinocytes. Interestingly,
inhibition of epidermal growth factor receptor signaling efficiently
blocks the increased Rac-GTP levels observed after contact
formation. We conclude that cadherin-dependent
adhesion can activate Rac via epidermal growth factor receptor signaling.
Rac Activation upon Cell-Cell Contact Formation Is Dependent on
Signaling from the Epidermal Growth Factor Receptor*
§,
*
This work was supported by the Cancer Research Campaign and
the Medical Research Council (Senior Research Fellowship to V. B.;
Postdoctoral Fellowship to J. K. Z.; Ph.D. studentship to M. B.).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.
Supported by a fellowship from the Ministerio de Ciencia y
Tecnología, Spain.
§
Present address: Cell and Molecular Biology Section, Division of
Biomedical Sciences, Faculty of Medicine, Imperial College, Sir
Alexander Fleming Bldg., Exhibition Rd., London SW7 2AZ, United Kingdom.
¶
To whom correspondence should be addressed. Tel.:
44-20-7594-3233; Fax: 44-20-7594-3015; E-mail: v.braga@ic.ac.uk.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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