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Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins

  • Kunihiko Hiraoka
  • , Kozo Kaibuchi
  • , Satoshi Ando
  • , Takashi Musha
  • , Kenji Takaishi
  • , Takakazu Mizuno
  • , Makoto Asada
  • , Luc Ménard
  • , Eric Tomhave
  • , John Didsbury
  • , Ralph Snyderman
  • , Yoshimi Takai

研究成果: ジャーナルへの寄稿学術論文査読

抄録

Six peaks of small GTP-binding proteins (G proteins) were separated by column chromatographies from the cytosol fraction of the differentiated HL-60 cells: two peaks of rho p21, one peak of smg rap1 p21, two peaks of rac1 p21, and one peak of an unidentified small G protein with a Mr of about 20,000 (20 KG). smg GDS, previously thought to be a stimulatory GDP GTP exchange protein for smg p21, Ki-ras p21, and rho p21, but not for Ha-ras p21 or smg p25A, was also active on rac1 p21. rho GDI, previously thought to be an inhibitory GDP GTP exchange protein specific for rho p21, was also active on rac1 p21. These results indicate that both smg GDS and rho GDI are active on multiple small G proteins.

本文言語英語
ページ(範囲)921-930
ページ数10
ジャーナルBiochemical and Biophysical Research Communications
182
2
DOI
出版ステータス出版済み - 31-01-1992
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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