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Bioessays. 2005 Apr;27(4):408-15.

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

Author information

1
Laboratoire de Biologie Moléculaie et Cellulaire de la Différenciation- INSERM U309 Equipe Chromatine et expression des gènes, Institut Albert Bonniot, Faculté de. Médecine-Pharmacie, 38706 La Tronche, France.

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.

PMID:
15770681
DOI:
10.1002/bies.20210
[Indexed for MEDLINE]

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