Glucose activation of the yeast plasma membrane H+‐ATPase requires the ubiquitin–proteasome proteolytic pathway

FEBS Letters

de la Fuente, Natalia¹  Maldonado, Ana M¹  Portillo, Francisco¹ 

[1] Departamento de Bioquı́mica, Facultad de Medicina, Universidad Autónoma de Madrid and Instituto de Investigaciones Biomédicas del Consejo Superior de Investigaciones Cientı́ficas, Arturo Duperier 4, E-28029 Madrid, Spain

关键词: H+-ATPase;    Plasma membrane;    Glucose activation;    Ubiquitin;    Saccharomyces cerevisiae;   

DOI  :  10.1016/S0014-5793(97)00721-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Glucose triggers transcriptional and post-transcriptional mechanisms that increase the level and activity of Saccharomyces cerevisiae plasma membrane H⁺-ATPase. We have studied the post-transcriptional activation of the enzyme by glucose and have found that Rsp5, a ubiquitin–protein ligase enzyme, Ubc4, a ubiquitin-conjugating enzyme, and the 26S proteasome complex are implicated in this activation. These results suggest that ATPase activation by glucose requires the ubiquitin–proteasome proteolytic pathway. This is supported by the fact that over-expression of the ubiquitin-specific protease Ubp2, which cleaves ubiquitin from its branched conjugates, inhibits this activation. We propose that glucose triggers degradation of an inhibitory protein resulting in enzyme activation.

【 授权许可】

Unknown