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Vol. 14, Issue 2, 658-669, February 2003
and
*Departments of Pediatrics and Pharmacology, University of
Wisconsin, Madison, Wisconsin 53706; and
Mammalian cDNA expression cloning was used to identify novel
regulators of integrin-mediated cell-substratum adhesions.
Using a focal adhesion morphology screen, we identified a cDNA with homology to a receptor for activated protein kinase C (RACK1) that
induced a loss of central focal adhesions and stress fibers in CHO-K1
cells. The identified cDNA was a C-terminal truncated form of RACK1
that had one of the putative protein kinase C binding sites but lacked
the region proposed to bind the Department of Molecular Cardiology, The
Cleveland Clinic Foundation, Cleveland, Ohio 44195
integrin cytoplasmic domain and the tyrosine kinase Src. To investigate the role of RACK1 during cell spreading and migration, we tagged RACK1, a C-terminal truncated RACK1 and a point mutant that does not bind Src
(RACK Y246F) with green fluorescent protein and expressed them in
CHO-K1 cells. We found that RACK1 regulates the organization of focal
adhesions and that it localizes to a subset of nascent focal complexes
in areas of protrusion that contain paxillin but not vinculin. We also
found that RACK1 regulates cell protrusion and chemotactic migration
through its Src binding site. Together, these findings suggest that
RACK1 regulates adhesion, protrusion, and chemotactic migration through
its interaction with Src.
Online
version of this article contains video material for some figures.
Online version available at www.molbiolcell.org.
Corresponding author. E-mail address:
huttenlocher{at}facstaff.wisc.edu.
§
Current address: Department of Zoology, University
of Wisconsin, Madison, Wisconsin 53706.
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