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Vol. 273, Issue 1, 9-12, January 2, 1998
1 Integrin Signaling Stimulates Tyrosine
Phosphorylation of p190RhoGAP and Membrane-protrusive
Activities at Invadopodia
,,, and
From the The ligation of available Lombardi Cancer Center & Department of Cell
Biology, Georgetown University Medical Center, Washington, D. C. 20007 and the ¶ Craniofacial Developmental Biology and Regeneration
Branch, NIDR, National Institutes of Health, Bethesda, Maryland
20892
6
1
integrin in adherent LOX melanoma cells by laminin G peptides and
integrin stimulatory antibodies induced cell invasiveness, independent
of adhesion activity of integrins that were pre-bound to extracellular
matrix (Nakahara, H., Nomizu, M., Akiyama, S. K., Yamada, Y., Yeh,
Y., and Chen, W.-T. (1996) J. Biol. Chem. 271, 27221-27224). Here, we show that this induced invasion involves an
increase in tyrosine phosphorylation of a 190-kDa GTPase-activating
protein for Rho family members (p190RhoGAP; p190) and
membrane-protrusive activities at invadopodia. This tyrosine
phosphorylation does not occur when the adherent cells are treated with
non-activating antibody against 1 integrin, control laminin
peptides, or tyrosine kinase inhibitors genistein and herbimycin A. Although p190 and F-actin co-distribute in all cell cortex extensions,
tyrosine-phosphorylated proteins including p190 appear to associate
with F-actin specifically in invadopodia. In addition, the localized
matrix degradation and membrane-protrusive activities were blocked by
treatment of LOX cells with tyrosine kinase inhibitors as well as
microinjection of antibodies directed against p190 but not by
non-perturbing antibodies or control buffers. We suggest that
activation of the 61 integrin signaling regulates the tyrosine
phosphorylation state of p190 which in turn connects downstream
signaling pathways through Rho family GTPases to actin cytoskeleton in
invadopodia, thus promoting membrane-protrusive and degradative
activities necessary for cell invasion.
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