The posttranslational processing of ras p21 is critical for its stimulation of yeast adenylate cyclase

H. Horiuchi, K. Kaibuchi, M. Kawamura, Y. Matsuura, N. Suzuki, Y. Kuroda, T. Kataoka, Y. Takai

研究成果: Article査読

25 被引用数 (Scopus)

抄録

Mammalian ras genes substitute for the yeast RAS gene, and their products activate adenylate cyclase in yeast cells, although the direct target protein of mammalian ras p21s remains to be identified. ras p21s undergo posttranslational processing, including prenylation, proteolysis, methylation, and palmitoylation, at their C-terminal regions. We have previously reported that the posttranslational processing of Ki-ras p21 is essential for its interaction with one of its GDP/GTP exchange proteins named smg GDS. In this investigation, we have studied whether the posttranslational processing of Ki- and Ha-ras p21s is critical for their stimulation of yeast adenylate cyclase in a cell-free system. We show that the posttranslationally fully processed Ki- and Ha-ras p21s activate yeast adenylate cyclase far more effectively than do the unprocessed proteins. The previous and present results suggest that the posttranslational processing of ras p21s is important for their interaction not only with smg GDS but also with the target protein.

本文言語English
ページ(範囲)4515-4520
ページ数6
ジャーナルMolecular and cellular biology
12
10
DOI
出版ステータスPublished - 1992
外部発表はい

ASJC Scopus subject areas

  • 分子生物学
  • 細胞生物学

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