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J. Biol. Chem., Vol. 277, Issue 15, 12487-12490, April 12, 2002
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1 Integrin-containing Invadopodia Promotes Cell
Invasion*
§,§,
From the In viral Src (v-Src)-transformed cells,
focal adhesion kinase (FAK) associates with v-Src by combined v-Src SH2
and gain-of-function v-Src SH3 domain binding to FAK. Here we assess
the significance of the Arg-95 to Trp gain-of-function mutation in the
v-Src SH3 domain through comparisons of Src Department of Immunology, The
Scripps Research Institute, La Jolla, California 92037 and the
¶ Department of Stomatology, University of California, San
Francisco, California 94143
/ fibroblasts
transformed with either Prague C v-Src or a point mutant (v-Src-RT)
containing a normal (Arg-95) SH3 domain. Both v-Src isoforms exhibited
equivalent kinase activity, enhanced Src/ cell motility, and
stimulated cell growth in both low serum and soft agar. The stability
of a v-Src·FAK signaling complex and FAK phosphorylation at
Tyr-861 and Tyr-925 were reduced in v-Src-RT- compared with
v-Src-transformed cells. v-Src but not v-Src-RT promoted Src/ cell
invasion through a reconstituted Matrigel basement membrane barrier and
v-Src co-localized with FAK and 
1 integrin at
invadopodia. In contrast, v-Src-RT exhibited a partial perinuclear and
focal contact distribution in Src/ cells.
Adenovirus-mediated FAK overexpression promoted v-Src-RT
recruitment to invadopodia, the formation of a v-Src-RT·FAK signaling
complex, and reversed the v-Src-RT invasion deficit. Adenovirus-mediated inhibition of FAK blocked v-Src-stimulated cell
invasion. These studies establish that gain-of-function v-Src SH3
targeting interactions with FAK at 1 integrin-containing invadopodia act to stabilize a v-Src·FAK signaling complex promoting cell invasion.
Supported by Grants from the National Institutes of Health. To
whom correspondence should be addressed: Dept. of Immunology, The
Scripps Research Inst., IMM26, 10550 N. Torrey Pines Rd., La Jolla, CA
92037. Tel.: 858-784-8207; Fax: 858-784-8227; E-mail: dschlaep@scripps.edu.
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