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(Received for publication, April 30, 1997, and in revised form, June 10, 1997)
From the Reduction of gap junctional communication in
v-src transformed cells is accompanied by tyrosine
phosphorylation of the gap junction protein, connexin 43 (Cx43). Cx43
is phosphorylated on tyrosine by v-Src. The Src homology 3 (SH3) and
Src homology 2 (SH2) domains of v-Src mediate interactions with
substrate proteins. SH3 domains interact with proline-rich peptide
motifs. SH2 domains associate with short amino acid sequences
containing phosphotyrosine. We present evidence that the SH3 and SH2
domains of v-Src bind to proline-rich motifs and a phosphorylated
tyrosine residue in the C-terminal tail of Cx43. Cx43 bound to the SH3
domain of v-Src, but not c-Src, in vitro.
Tyrosine-phosphorylated Cx43 bound to the SH2 domain of v-Src in
vitro. v-Src coprecipitated with Cx43 from
v-src-transformed Rat-1 fibroblasts. Mutations in the SH3 and SH2 domains of v-Src, and in the proline-rich region or tyrosine 265 of Cx43, reduced interactions between v-Src and Cx43 in
vivo. Tyrosine phosphorylation of Cx43 was dependent on the
association of v-Src and Cx43. These results provide further evidence
for the direct involvement of v-Src in tyrosine phosphorylation of Cx43
and inhibition of gap junctional communication in
v-src-transformed cells.
Volume 272, Number 36,
Issue of September 5, 1997
pp. 22824-22831
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Molecular Biology and Virology Laboratory,
The Salk Institute for Biological Studies, La Jolla, California 92037 and § Molecular Carcinogenesis, Cancer Research Center of
Hawaii, University of Hawaii at Manoa, Honolulu, Hawaii 96813
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