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(Received for publication, February 29, 1996, and in revised form, April 29, 1996)
From the Differentiation Programme, European Molecular Biology
Laboratory, Meyerhofstrasse 1, 69012 Heidelberg, Federal Republic of Germany
The Src family of protein tyrosine kinases has
been implicated in the response of cells to platelet-derived growth
factor (PDGF) or epidermal growth factor (EGF). We recently described a
microinjection approach that we used to demonstrate that kinase
activity of Src family members is required for PDGF- and EGF-induced
S-phase entry of fibroblasts. We have now used this approach to ask
whether a functional SH3 domain of Src is required to transduce the
mitogenic signal upon PDGF or EGF stimulation. Microinjection of
plasmids encoding Src mutants lacking the SH3 domain (Src
Volume 271, Number 28,
Issue of July 12, 1996
pp. 16807-16812
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
SH3) or
point-mutated within the ligand binding surface of the SH3 domain, but
with intact kinase domains, inhibited the mitogenic effect of PDGF and
EGF in fibroblasts. SrcSH3 could still associate with the PDGF
receptor, suggesting that the inhibitory effect of the Src SH3 mutants
was brought about by a failure of the PDGF receptor·SrcSH3 complex
to relay the mitogenic signal further downstream. Chimeric molecules in
which the Src SH3 domain was replaced with that of spectrin or Lck also
blocked PDGF-induced DNA synthesis, whereas a chimera containing the
Fyn SH3 domain did not. These data suggest that the Src or Fyn SH3
domain is required either for correct substrate selection or to recruit
other proteins to the PDGF receptor.
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