BRCA1 ubiquitylation of CtIP: Just the tIP of the iceberg?

被引：14

作者：

Barber, Louise J. ^{[1
]}

Boulton, Simon J. ^{[1
]}

机构：

[1] London Res Inst, Clare Hall Labs, Canc Res UK, DNA Damage Response Lab, S Mimms EN6 3LD, Herts, England

来源：

DNA REPAIR | 2006年 / 5卷 / 12期

关键词：

CtIP; BRCA1; ubiquitylation; E3-ubiquitin ligase;

D O I：

10.1016/j.dnarep.2006.08.009

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Ubiquitylation is an important regulatory mechanism of many cellular processes. The breast and ovarian cancer-specific tumour suppressor BRCA1 is well acknowledged to be a RING/E3 ubiquitin ligase, however, identification of its physiological substrates has proved elusive. Recently published data have shown that the BRCA1-interacting protein CtIP is in fact ubiquitylated by BRCA1, and opens new avenues for the isolation of other substrate proteins. (c) 2006 Elsevier B.V. All rights reserved.

引用

页码：1499 / 1504

页数：6

共 54 条

[51] The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repression [J].