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

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Abstract

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.

Original languageEnglish
Pages (from-to)921-930
Number of pages10
JournalBiochemical and Biophysical Research Communications
Volume182
Issue number2
DOIs
Publication statusPublished - 31-01-1992

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Hiraoka, K., Kaibuchi, K., Ando, S., Musha, T., Takaishi, K., Mizuno, T., Asada, M., Ménard, L., Tomhave, E., Didsbury, J., Snyderman, R., & Takai, Y. (1992). Both stimulatory and inhibitory GDP GTP exchange proteins, smg GDS and rho GDI, are active on multiple small GTP-binding proteins. Biochemical and Biophysical Research Communications, 182(2), 921-930. https://doi.org/10.1016/0006-291X(92)91820-G