Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability
✍ Scribed by Cécile Caron; Cyril Boyault; Saadi Khochbin
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 169 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0265-9247
No coin nor oath required. For personal study only.
✦ Synopsis
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.