The large N-terminal domain of Cdc25 protein of the yeast Saccharomyces cerevisiae is required for glucose-induced Ras2 activation

被引：11

作者：

Paiardi, Chiara ^{[1
]}

Belotti, Fiorella ^{[1
]}

Colombo, Sonia ^{[1
]}

Tisi, Rentata ^{[1
]}

Martegani, Enzo ^{[1
]}

机构：

[1] Univ Milano Bicocca, Dept Biotechnol & Biosci, I-20126 Milan, Italy

来源：

FEMS YEAST RESEARCH | 2007年 / 7卷 / 08期

关键词：

Cdc25; RasGTP; cAMP; Saccharomyces cerevisiae;

D O I：

10.1111/j.1567-1364.2007.00300.x

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The Saccharomyces cerevisiae CDC25 gene encodes a guanine nucleotide exchange factor for Ras proteins whose catalytic domain is highly homologous to Ras-guanine nucleotide exchange factors from higher eukaryotes. In this study, glucose-induced Ras activation and cAMP response were investigated in mutants lacking the N-terminal domain of Cdc25 or where the entire CDC25 coding sequence was substituted by an expression cassette for a mammalian guanine nucleotide exchange factor catalytic domain. Our results suggest that an unregulated, low Ras guanine nucleotide exchange factor activity allows a normal glucose-induced cAMP signal that appears to be mediated mainly by the Gpr1/Gpa2 system, but it was not enough to sustain the glucose-induced increase of Ras2-GTP normally observed in a wild-type strain.

引用

页码：1270 / 1275

页数：6

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