Partial purification and characterization of GDP dissociation stimulator (GDS) for the rho proteins from bovine brain cytosol

Mitsuo Isomura, Kozo Kaibuchi, Takeshi Yamamoto, Shiro Kawamura, Masaya Katayama, Yoshimi Takai

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)

Abstract

A novel type of regulatory proteins for the rho proteins (rhoA p21 and rhoB p20), ras p21-like small GTP-binding proteins (G proteins), are partially purified from bovine brain cytosol. These regulatory proteins, named rho GDP dissociation stimulator (GDS)1 and -2, stimulate the dissociation of GDP from rhoA p21 and rhoB p20. rho GDS1 and -2 are inactive for other ras p21/ras p21-like small G proteins including c-Ha-ras p21, smg p21B, and smg p25A. Since we have previously shown that the rate limiting step for the GDP GTP exchange reaction of the rho proteins is the dissociation of GDP from these proteins, the present results suggest that rho GDS1 and -2 stimulate the GDP GTP exchange reaction of the rho proteins. rho GDS1 and -2 are distinct from the GAP- and GDI-types of regulatory proteins for the rho proteins previously purified from bovine brain cytosol. rho GAP stimulates the GTPase activity of the rho proteins and rho GDI inhibits the GDP GTP exchange reaction of the rho proteins. The present results together with these earlier observations indicate that the rho proteins are regulated by at least three different types of regulatory proteins, GDS, GDI, and GAP.

Original languageEnglish
Pages (from-to)652-659
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume169
Issue number2
DOIs
Publication statusPublished - 15-06-1990
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Partial purification and characterization of GDP dissociation stimulator (GDS) for the rho proteins from bovine brain cytosol'. Together they form a unique fingerprint.

Cite this