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J Biol Chem, Vol. 275, Issue 6, 3741-3744, February 11, 2000
From the Departments of Molecular Pharmacology and of
We have studied the role of phosphatidylinositol
3-kinases (PI 3-kinases) in the regulation of the actin cytoskeleton in
MTLn3 rat adenocarcinoma cells. Stimulation of MTLn3 cells with
epidermal growth factor (EGF)
induced a rapid increase in actin polymerization, with production of
lamellipodia within 3 min. EGF-stimulated lamellipodia were blocked by
100 nM wortmannin, suggesting the involvement of a
class Ia PI 3-kinase. MTLn3 cells contain equal amounts of p110
ACCELERATED PUBLICATION
Specific Requirement for the p85-p110
Phosphatidylinositol
3-Kinase during Epidermal Growth Factor-stimulated Actin Nucleation
in Breast Cancer Cells*
,,§, and Anatomy and Structural Biology, Albert Einstein College
of Medicine, Bronx, New York 10461
and
p110
, and do not contain p110
. Injection of specific inhibitory
antibodies to p110 induced cell rounding and blocked EGF-stimulated
lamellipod extension, whereas control or anti-p110 antibodies had no
effect. In contrast, both antibodies inhibited EGF-stimulated DNA
synthesis. An in situ assay for actin nucleation showed
that EGF-stimulated formation of new barbed ends was blocked by
injection of anti-p110 antibodies. In summary, the p110 isoform of PI 3-kinase is specifically required for EGF-stimulated actin nucleation during lamellipod extension in breast cancer cells.
*
This work was supported by a Scholar Award from the Irma T. Hirschl Trust and National Institutes of Health Grant GM55692 (to
J. M. B.) and by a grant from the United States Army (to J. E. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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