Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J Biol Chem 1997 Sep 12;272(37):23371-5
Date
09/12/1997Pubmed ID
9287351DOI
10.1074/jbc.272.37.23371Scopus ID
2-s2.0-0030846295 (requires institutional sign-in at Scopus site) 369 CitationsAbstract
The Rho GDP dissociation inhibitor (GDI) forms a complex with the GDP-bound form of the Rho family small G proteins and inhibits their activation. The GDP-bound form complexed with Rho GDI is not activated by the GDP/GTP exchange factor for the Rho family members, suggesting the presence of another factor necessary for this activation. We have reported that the Rho subfamily members regulate the ezrin/radixin/moesin (ERM)-CD44 system, implicated in reorganization of actin filaments. Here we report that Rho GDI directly interacts with ERM, initiating the activation of the Rho subfamily members by reducing the Rho GDI activity. These results suggest that ERM as well as Rho GDI and the Rho GDP/GTP exchange factor are involved in the activation of the Rho subfamily members, which then regulate reorganization of actin filaments through the ERM system.
Author List
Takahashi K, Sasaki T, Mammoto A, Takaishi K, Kameyama T, Tsukita S, Takai YAuthor
Akiko Mammoto MD, PhD Associate Professor in the Pediatrics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ActinsBlood Proteins
Cytoskeletal Proteins
Cytoskeleton
GTP-Binding Proteins
Guanine Nucleotide Dissociation Inhibitors
Hyaluronan Receptors
Membrane Proteins
Microfilament Proteins
Peptide Fragments
Phosphoproteins
Protein Binding
Proteins
Recombinant Fusion Proteins
rab3 GTP-Binding Proteins
rho GTP-Binding Proteins
rho-Specific Guanine Nucleotide Dissociation Inhibitors
