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J Biol Chem, Vol. 274, Issue 30, 21430-21436, July 23, 1999
Department of Cell Biology and Neuroscience, University of Texas
Southwestern Medical Center, Dallas, Texas 75235-9039
Rac1 and RhoA regulate membrane ruffling and
stress fiber formation. Both molecules appear to exert their control
from the plasma membrane. In fibroblasts stimulated with
platelet-derived growth factor or lysophosphatidic acid, the
reorganization of the cytoskeleton begins at specific sites on the cell
surface. We now report that endogenous Rac1 and RhoA also have a
polarized distribution at the cell surface. Cell fractionation and
immunogold labeling show that in quiescent fibroblasts both of these
molecules are concentrated in caveolae, which are plasma membrane
domains that are associated with actin-rich regions of the cell.
Treatment of these cells with platelet-derived growth factor stimulated the recruitment of additional Rac1 and RhoA to caveolae fractions, while lysophosphatidic acid only caused the recruitment of RhoA. We
could reconstitute the recruitment of RhoA using either whole cell
lysates or purified caveolae. Surprisingly, pretreatment of the lysates
with exoenzyme C3 shifted both resident and recruited RhoA from
caveolae to noncaveolae membranes. The shift in location was not caused
by inactivation of the RhoA effector domain. Moreover, chimeric
proteins containing the C-terminal consensus site for Rac1 and RhoA
prenylation were constitutively targeted to caveolae fractions. These
results suggest that the polarized distribution of Rho family proteins
at the cell surface involves an initial targeting of the protein to
caveolae and a mechanism for retaining it at this site.
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C. Gomez-Mouton, J. L. Abad, E. Mira, R. A. Lacalle, E. Gallardo, S. Jimenez-Baranda, I. Illa, A. Bernad, S. Manes, and C. Martinez-A. From the Cover: Segregation of leading-edge and uropod components into specific lipid rafts during T cell polarization PNAS, August 14, 2001; 98(17): 9642 - 9647. [Abstract] [Full Text] [PDF]
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