Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability

被引：229

作者：

Caron, C ^{[1
]}

Boyault, C ^{[1
]}

Khochbin, S ^{[1
]}

机构：

[1] INSERM, Lab Biol Mol & Cellulaire Differenciat, Inst Albert Bonniot, Equipe Chromatine & Express Genes,Fac Med Pharm,U, F-38706 La Tronche, France

来源：

BIOESSAYS | 2005年 / 27卷 / 04期

关键词：

D O I：

10.1002/bies.20210

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：

It is now becoming apparent that cross-talk between two protein lysine modifications, acetylation and ubiquitination, is a critical regulatory mechanism controlling vital cellular functions. The most apparent effect is the inhibition of proteasome-mediated protein degradation by lysine acetylation. Analysis of the underlying mechanisms, however, shows that, besides a direct competition between the two lysine modifications, more complex and indirect processes also connect these two signalling pathways. These findings point to protein lysine acetylation as a potential regulator of various cellular functions involving protein ubiquitination. (c) 2005 Wiley Periodicals, Inc.

引用

页码：408 / 415

页数：8

共 74 条

[1] Potentiation of tumor necrosis factor-induced NF-κB activation by deacetylase inhibitors is associated with a delayed cytoplasmic reappearance of IκBα [J].