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Vol. 273, Issue 3, 1689-1698, January 16, 1998
From the To survive in a mechanically active environment,
cells must adapt to variations of applied membrane tension. A
collagen-coated magnetic bead model was used to apply forces directly
to the actin cytoskeleton through integrin receptors. We demonstrate
here that by a calcium-dependent mechanism, human fibroblasts reinforce locally their connection with extracellular adhesion sites by inducing
actin assembly and by recruiting actin-binding protein 280 (ABP-280)
into cortical adhesion complexes. ABP-280 was phosphorylated on serine
residues as a result of force application. This phosphorylation and the
force-induced actin reorganization were largely abrogated by inhibitors
of protein kinase C. In a human melanoma cell line that does not
express ABP-280, actin accumulation could not be induced by force,
whereas in stable transfectants expressing ABP-280, force-induced actin
accumulation was similar to human fibroblasts. Cortical actin assembly
played a role in regulating the activity of stretch-activated,
calcium-permeable channels (SAC) since sustained force application
desensitized SAC to subsequent force applications, and the decrease in
stretch sensitivity was reversed after treatment with cytochalasin D. ABP-280-deficient cells showed a >90% increase in cell death compared
with ABP-280+ve cells after force application. We conclude that ABP-280
plays an important role in mechanoprotection by reinforcing the
membrane cortex and desensitizing SACs.
The Role of Actin-binding Protein 280 in
Integrin-dependent Mechanoprotection
,,,
, and
MRC Group in Periodontal Physiology, Faculty
of Dentistry, University of Toronto,
Toronto, Ontario M5S 1A8, Canada, the ¶ Brigham and Women's
Hospital, Harvard Medical School, Boston, Massachusetts 02115, and
the Faculty of Medicine, Department of Medicine, University of
Toronto, Toronto, Ontario M5S 1A8, Canada
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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