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Regulatory cross‐talk between lysine acetylation and ubiquitination: role in the control of protein stability
Author(s) -
Caron Cécile,
Boyault Cyril,
Khochbin Saadi
Publication year - 2005
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.20210
Subject(s) - lysine , acetylation , ubiquitin , proteasome , regulator , microbiology and biotechnology , chemistry , biochemistry , biology , amino acid , gene
Abstract 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. BioEssays 27:408–415, 2005. © 2005 Wiley periodicals, Inc.