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

研究成果: Article査読

26 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)1095-1102
ページ数8
ジャーナルBiochemical and Biophysical Research Communications
174
3
DOI
出版ステータスPublished - 14-02-1991
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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