Back to Search
Start Over
Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
- Source :
- The Journal of biological chemistry. 272(37)
- Publication Year :
- 1997
-
Abstract
- 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.
- Subjects :
- rho GTP-Binding Proteins
GTP'
Moesin
Recombinant Fusion Proteins
rab3 GTP-Binding Proteins
Small G Protein
macromolecular substances
Biochemistry
Ezrin
Radixin
GTP-Binding Proteins
RHO protein GDP dissociation inhibitor
rho-Specific Guanine Nucleotide Dissociation Inhibitors
Molecular Biology
Cytoskeleton
Guanine Nucleotide Dissociation Inhibitors
Chemistry
Microfilament Proteins
Membrane Proteins
Proteins
Cell Biology
Blood Proteins
Phosphoproteins
Actins
Peptide Fragments
Cell biology
Cytoskeletal Proteins
Hyaluronan Receptors
MDia1
Protein Binding
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 272
- Issue :
- 37
- Database :
- OpenAIRE
- Journal :
- The Journal of biological chemistry
- Accession number :
- edsair.doi.dedup.....561a6b0de782320af9e4f24fcda03d82