The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2

被引：234

作者：

Kamura, T

Conrad, MN

Yan, Q

Conaway, RC

Conaway, JW

机构：

[1] Oklahoma Med Res Fdn, Howard Hughes Med Inst, Oklahoma City, OK 73104 USA

[2] Oklahoma Med Res Fdn, Program Mol & Cell Biol, Oklahoma City, OK 73104 USA

[3] Univ Oklahoma, Hlth Sci Ctr, Dept Biochem & Mol Biol, Oklahoma City, OK 73190 USA

来源：

GENES & DEVELOPMENT | 1999年 / 13卷 / 22期

关键词：

Rbx1; ROC1; Hrt1; SCF; vonHippel-lindau; ubiquitin ligase; cullin; Rub1; NEDD8;

D O I：

10.1101/gad.13.22.2928

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The RING-H2 finger protein Rbx1 is a subunit of the related SCF ((S) under bar kp1-(C) under bar dc53/Cul1-(F) under bar-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/ Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5. Here we demonstrate that the Cdc53/Rbx1 and Cul2/Rbx1 modules also activate conjugation of the ubiquitin-like protein Rub1 to Cdc53 and Cul2 by the dedicated E2 Rub1 conjugating enzyme Ubc12. Our findings identify Rbx1 as a common component of enzyme systems responsible for ubiquitin and Rub1 modification of target proteins.

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收藏

页码：2928 / 2933

页数：6

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