Possible involvement of RAS-encoded proteins in glucose-induced inositolphospholipid turnover in Saccharomyces cerevisiae

K. Kaibuchi, A. Miyajima, K. I. Arai, K. Matsumoto

研究成果: Article査読

93 被引用数 (Scopus)

抄録

Incubation of yeast Saccharomyces cerevisiae at very low (0.02%) glucose levels led to arrest of the cell cycle at the G0/G1 phase. Readdition of glucose to these 'starved' yeast resulted in cell proliferation. In glucose-starved yeast, glucose stimulated 32P incorporation into phosphatidic acid, phosphatidylinositol, phosphatidylinositol monophosphate, and phosphatidylinositol bisphosphate but not into phosphatidylethanolamine and phosphatidylcholine. Preincubation of yeast with [3H]inositol and subsequent exposure to glucose resulted in rapid formation of [3H]inositol monophosphate and [3H]inositol trisphosphate, presumably derived from phosphatidylinositol and phosphatidylinositol bisphosphate. Under similar conditions, glucose elicited both efflux and influx of Ca2+ in yeast. Glucose-induced 32P incorporation into inositolphospholipids and formation of [3H]inositol phosphates were more pronounced in RAS-related mutants such as ras1, ras1 ras2 bcy1, and RAS2(Val)19 than in the wild-type strain. These results strongly suggest that glucose stimulates inositolphospholipid turnover, Ca2+ mobilization, and subsequent cell proliferation in a manner similar to that of growth factors with mammalian cells, and that RAS-encoded proteins are involved in regulation of this glucose-induced inositolphospholipid turnover in yeast.

本文言語English
ページ(範囲)8172-8176
ページ数5
ジャーナルProceedings of the National Academy of Sciences of the United States of America
83
21
DOI
出版ステータスPublished - 1986
外部発表はい

All Science Journal Classification (ASJC) codes

  • General

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