TY - JOUR
T1 - Conformational activation of radixin by G13 protein α subunit
AU - Vaiskunaite, Rita
AU - Adarichev, Vyacheslav
AU - Furthmayr, Heinz
AU - Kozasa, Tohru
AU - Gudkov, Andrei
AU - Voyno-Yasenetskaya, Tatyana A.
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 2000/8/25
Y1 - 2000/8/25
N2 - G13 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 Gα13. Interaction between radixin and Gα13 was confirmed by in vitro binding assay and by co-immunoprecipitation technique. Activated Gα13 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 Gα13-induced focus formation of Rat-1 fibroblasts but did not affect Ras-induced focus formation. Our resets identifying a new signaling pathway for Gα13 indicate that ERM proteins can be activated by and serve as effectors of heterotrimeric G proteins.
AB - G13 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 Gα13. Interaction between radixin and Gα13 was confirmed by in vitro binding assay and by co-immunoprecipitation technique. Activated Gα13 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 Gα13-induced focus formation of Rat-1 fibroblasts but did not affect Ras-induced focus formation. Our resets identifying a new signaling pathway for Gα13 indicate that ERM proteins can be activated by and serve as effectors of heterotrimeric G proteins.
UR - http://www.scopus.com/inward/record.url?scp=0034714347&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034714347&partnerID=8YFLogxK
U2 - 10.1074/jbc.M001863200
DO - 10.1074/jbc.M001863200
M3 - Article
C2 - 10816569
AN - SCOPUS:0034714347
VL - 275
SP - 26206
EP - 26212
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 34
ER -