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

@article{Caron2005RegulatoryCB,
  title={Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability.},
  author={C{\'e}cile Caron and Cyril Boyault and Saadi Khochbin},
  journal={BioEssays : news and reviews in molecular, cellular and developmental biology},
  year={2005},
  volume={27 4},
  pages={408-15}
}
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… CONTINUE READING

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