Stoichiometric interaction of smg p21 with its GDP GTP exchange protein and its novel action to regulate the translocation of smg p21 between membrane and cytoplasm

Shiro Kawamura, Kozo Kaibuchi, Motoki Hiroyoshi, Yutaka Hata, Yoshimi Takai

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

We have previously purified a GDP GTP exchange protein for smg p21A and -B, members of a ras p21 ras p21-like small GTP-binding protein superfamily. This regulatory protein, named smg p21 GDP dissociation stimulator (GDS), stimulates the dissociation of both GDP and GTP from and the subsequent binding of both GDP and GTP to smg p21s. We show here that smg p21 GDS forms a complex with both the GDP- and GTP-bound forms of smg p21B at a molar ratio of about 1:1. Both the GDP- and GTP-bound forms of smg p21B bound to membranes. smg p21 GDS inhibited this binding and moreover induced the dissociation of the prebound smg p21B from the membranes. These results indicate that smg p21 GDS stoichiometrically interacts with smg p21B and thereby regulates its GDP GTP exchange reaction and its translocation between membranes and cytoplasm.

Original languageEnglish
Pages (from-to)1095-1102
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume174
Issue number3
DOIs
Publication statusPublished - 14-02-1991
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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