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.
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收藏
页码：408 / 415
页数：8
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