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Vol. 13, No. 18, pp. 2400-2411, September 15, 1999
1 Department of Pharmacology and Cancer Biology, Duke
University Medical Center, Durham, North Carolina 27710 USA;
4 Shepens Eye Research Institute, Harvard Medical School,
Boston, Massachusetts 02114 USA
The c-Abl tyrosine kinase localizes to the cytoplasm and plasma
membrane in addition to the nucleus. However, there is little information regarding a role for c-Abl in the
cytoplasm/plasma membrane compartments. Here we report
that a membrane pool of c-Abl is activated by the growth factors PDGF
and EGF in fibroblasts. The pattern and kinetics of activation are
similar to growth factor activation of Src family kinases. To determine
whether a link existed between activation of c-Abl and members of the
Src family, we examined c-Abl kinase activity in cells that expressed
oncogenic Src proteins. We found that c-Abl kinase activity was
increased by 10- to 20-fold in these cells, and that Src and Fyn
kinases directly phosphorylated c-Abl in vitro. Furthermore,
overexpression of wild-type Src potentiated c-Abl activation by growth
factors, and a kinase-inactive form of Src reduced this activation,
showing that Abl activation by growth factors occurs at least in part via activation of Src kinases. Significantly, we show that c-Abl has a
functional role in the morphological response to PDGF. Whereas PDGF
treatment of serum-starved wild-type mouse embryo fibroblasts resulted
in distinct linear or circular/dorsal membrane ruffling, c-Abl-null cells demonstrated dramatically reduced ruffling in response
to PDGF, which was rescued by physiological re-expression of c-Abl.
These data identify c-Abl as a downstream target of activated receptor
tyrosine kinases and Src family kinases, and show for the first time
that c-Abl functions in the cellular response to growth factors.
[Key Words: c-Abl; Src; receptor tyrosine kinases; cytoskeleton]
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