Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl. Oncogene 1998 Jun 25;16(25):3279-84
Date
07/29/1998Pubmed ID
9681826DOI
10.1038/sj.onc.1201874Scopus ID
2-s2.0-0032566011 (requires institutional sign-in at Scopus site) 105 CitationsAbstract
The Rho small G protein family, consisting of the Rho, Rac, and Cdc42 subfamilies, regulates various actin cytoskeleton-dependent cell functions. The Rho subfamily members regulate ERM (ezrin, radixin and moesin)-dependent association of the actin cytoskeleton with the plasma membrane. Moreover, the N-terminal regions of ERM interact with Rho GDI, an inhibitory regulator of all the Rho family members, and reduce its inhibitory action, finally initiating the activation of the Rho family members. We show here that the N-terminal region of radixin furthermore interacts with Dbl, a stimulatory GDP/GTP exchange protein of the Rho family members. This interaction does not affect the Dbl activity to stimulate the GDP/GTP exchange reaction of RhoA, a member of the Rho subfamily. Dbl does not interact with radixin which is precomplexed with Rho GDI, and Rho GDI displaces Dbl from radixin. Thus, radixin plays an important role in activation of the Rho family members by recruiting their positive and negative regulators.
Author List
Takahashi K, Sasaki T, Mammoto A, Hotta I, Takaishi K, Imamura H, Nakano K, Kodama A, 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
Binding SitesBlood Proteins
Cytoskeletal Proteins
DNA-Binding Proteins
GTP-Binding Proteins
Glutathione Transferase
Guanine Nucleotide Dissociation Inhibitors
Guanosine Diphosphate
Guanosine Triphosphate
Membrane Proteins
Peptide Fragments
Protein Binding
Retroviridae Proteins, Oncogenic
Rho Factor
Transcription Factors
rho-Specific Guanine Nucleotide Dissociation Inhibitors
