Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability.
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.
Caron
Cécile
C
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.
Boyault
Cyril
C
Khochbin
Saadi
S
D000107:Acetylation; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases / Q000378:metabolism; D008239:Lysine / Q000737:chemistry / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology; D025801:Ubiquitin / Q000378:metabolism*
D056572:Histone Deacetylase Inhibitors; D011506:Proteins; D025801:Ubiquitin; D046988:Proteasome Endopeptidase Complex; D006655:Histone Deacetylases; D008239:Lysine