Conformational activation of radixin by G13 protein alpha subunit.
G(13) protein, one of the heterotrimeric guanine nucleotide-binding proteins (G proteins), regulates diverse and complex cellular responses by transducing signals from the cell surface presumably involving more than one pathway. Yeast two-hybrid screening of a mouse brain cDNA library identified radixin, a member of the ERM family of three closely ... related proteins (ezrin, radixin, and moesin), as a protein that interacted with Galpha(13). Interaction between radixin and Galpha(13) was confirmed by in vitro binding assay and by co-immunoprecipitation technique. Activated Galpha(13) induced conformational activation of radixin, as determined by binding of radixin to polymerized F-actin and by immunofluorescence in intact cells. Finally, two dominant negative mutants of radixin inhibited Galpha(13)-induced focus formation of Rat-1 fibroblasts but did not affect Ras-induced focus formation. Our results identifying a new signaling pathway for Galpha(13) indicate that ERM proteins can be activated by and serve as effectors of heterotrimeric G proteins.
Mesh Terms:
3T3 Cells, Animals, Blood Proteins, Cytoskeletal Proteins, GTP-Binding Protein alpha Subunits, G12-G13, Heterotrimeric GTP-Binding Proteins, Membrane Proteins, Mice, Microfilament Proteins, Microscopy, Confocal, Phosphoproteins, Protein Binding, Protein Conformation, Signal Transduction, Yeasts
3T3 Cells, Animals, Blood Proteins, Cytoskeletal Proteins, GTP-Binding Protein alpha Subunits, G12-G13, Heterotrimeric GTP-Binding Proteins, Membrane Proteins, Mice, Microfilament Proteins, Microscopy, Confocal, Phosphoproteins, Protein Binding, Protein Conformation, Signal Transduction, Yeasts
J. Biol. Chem.
Date: Aug. 25, 2000
PubMed ID: 10816569
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