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Vol. 9, Issue 2, 403-419, February 1998
¶
*Center for Cancer Research, Department of Biology, Massachusetts
Institute of Technology, Cambridge, Massachusetts 12139; and
The ERM proteins (ezrin, radixin, and moesin) are a group of band
4.1-related proteins that are proposed to function as
membrane/cytoskeletal linkers. Previous biochemical studies have
implicated RhoA in regulating the association of ERM proteins with
their membrane targets. However, the specific effect and mechanism of
action of this regulation is unclear. We show that lysophosphatidic
acid stimulation of serum-starved NIH3T3 cells resulted in
relocalization of radixin into apical membrane/actin protrusions, which
was blocked by inactivation of Rho by C3 transferase. An activated
allele of RhoA, but not Rac or CDC42Hs, was sufficient to induce apical membrane/actin protrusions and localize radixin or moesin into these
structures in both Rat1 and NIH3T3 cells. Lysophosphatidic acid
treatment led to phosphorylation of radixin preceding its redistribution into apical protrusions. Significantly, cotransfection of RhoAV14 or C3 transferase with radixin and moesin revealed that RhoA
activity is necessary and sufficient for their phosphorylation. These
findings reveal a novel function of RhoA in reorganizing the apical
actin cytoskeleton and suggest that this function may be mediated
through phosphorylation of ERM proteins.
Howard Hughes Medical Institute, Cambridge,
Massachusetts 02139
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