The Cdc48-Ufd1-Np14 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase

被引：12

作者：

Barbin, Lise ^{[1
]}

Eisele, Frederik ^{[1
]}

Santt, Olivier ^{[1
]}

Wolf, Dieter H. ^{[1
]}

机构：

[1] Univ Stuttgart, Inst Biochem, D-70569 Stuttgart, Germany

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2010年 / 394卷 / 02期

关键词：

Protein degradation; Gluconeogenesis; Fructose-1,6-bisphosphatase; Cdc48; complex; Polyubiquitination; Proteasome; YEAST SACCHAROMYCES-CEREVISIAE; AAA ATPASE CDC48/P97; ENDOPLASMIC-RETICULUM; PROTEIN-DEGRADATION; PHOSPHOENOLPYRUVATE CARBOXYKINASE; TRANSCRIPTION FACTOR; UBX DOMAIN; INACTIVATION; ER; CHAPERONE;

D O I：

10.1016/j.bbrc.2010.03.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The switch from gluconeogenesis to glycolysis in yeast has been shown to require ubiquitin-proteasome dependent elimination of the key enzyme fructose-1,6-bisphosphatase (FBPase). Prior to proteasomal degradation, polyubiquitination of the enzyme occurs via the ubiquitin-conjugating enzymes Ubc1, Ubc4, Ubc5 and Ubc8 in conjunction with a novel multi-subunit ubiquitin ligase, the Gid complex. As an additional machinery required for the catabolite degradation process, we identified the trimeric Cdc48(Ufd1-Np14) complex and the ubiquitin receptors Dsk2 and Rad23. We show that this machinery acts between polyubiquitination of FBPase and its degradation by the proteasome. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：335 / 341

页数：7

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