Degadration of mismatch repair hMutSα heterodimer by the ubiquitin-proteasome pathway

被引：23

作者：

Hernandez-Pigeon, H

Laurent, G

Humbert, O

Salles, B

Lautier, D

机构：

[1] Inst Claudius Regaud, Ctr Physiopathol Toulouse Purpan, INSERM, U563, F-31052 Toulouse, France

[2] Hop Purpan, Serv Hematol, F-31059 Toulouse, France

[3] CNRS, UMR 5089, Inst Pharmacol & Biol Struct, F-31077 Toulouse, France

来源：

FEBS LETTERS | 2004年 / 562卷 / 1-3期

关键词：

MSH2; MSH6; ubiquitination; protein stability; mismatch repair; proteasome;

D O I：

10.1016/S0014-5793(04)00181-4

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：

Mismatch repair plays a critical role in genome stability. This process requires several proteins including hMSH2/hMSH6 (hMutSalpha) heterodimer involved in the first stage of the process, the mispair recognition. We previously reported that in U937 and HL-60 cell lines, hMSH2 and hMSH6 protein expression was much lower than that in HeLa and KG1a cells. Here, we showed that the decreased expression of hMutSalpha results from differences in the degradation rate of both proteins by the ubiquitin-proteasome pathway. Our data suggest that in human cell lines, ubiquitin-proteasome could play an important role in the regulation of hMutSalpha protein expression, thereby regulating mismatch repair activity. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：40 / 44

页数：5

共 21 条

[1] Induction of two DNA mismatch repair proteins, MSH2 and MSH6, in differentiated human neuroblastoma SH-SY5Y cells exposed to doxorubicin [J].