CRL4s: the CUL4-RING E3 ubiquitin ligases

被引：326

作者：

Jackson, Sarah ^{[1
]}

Xiong, Yue ^{[1
]}

机构：

[1] Univ N Carolina, Lineberger Comprehens Canc Ctr, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2009年 / 34卷 / 11期

关键词：

DNA-BINDING PROTEIN; PIGMENTOSUM GROUP-E; VIRUS X-PROTEIN; LINKED MENTAL-RETARDATION; PARAMYXOVIRUS-V PROTEIN; CELL NUCLEAR ANTIGEN; E GENE-PRODUCT; DAMAGED DNA; SCHIZOSACCHAROMYCES-POMBE; S-PHASE;

D O I：

10.1016/j.tibs.2009.07.002

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 evolutionarily conserved cullin family proteins can assemble as many as 400 distinct E3 ubiquitin ligase complexes that regulate diverse cellular pathways. CUL4, one of three founding cullins conserved from yeast to humans, uses a large beta-propeller protein, DDB1, as a linker to interact with a subset of WD40 proteins that serve as substrate receptors, forming as many as 90 E3 complexes in mammals. Many CRL4 complexes are involved in chromatin regulation and are frequently hijacked by different viruses.

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页码：562 / 570

页数：9

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