Cellular and Molecular Life Sciences

, Volume 67, Issue 18, pp 3073–3087

Protein deacetylation by sirtuins: delineating a post-translational regulatory program responsive to nutrient and redox stressors


DOI: 10.1007/s00018-010-0402-y

Cite this article as:
Bao, J. & Sack, M.N. Cell. Mol. Life Sci. (2010) 67: 3073. doi:10.1007/s00018-010-0402-y


Lysine acetylation/deacetylation is increasingly being recognized as common post-translational modification that appears to be broadly operational throughout the cell. The functional roles of these modifications, outside of the nucleus, have not been extensively studied. Moreover, as acetyl-CoA donates the acetyl group for acetylation, nutrient availability and energetic status may be pivotal in this modification. Similarly, nutrient limitation is associated with the deacetylation reaction. This modification is orchestrated by a novel family of sirtuin deacetylases that function in a nutrient and redox dependent manner and targets non-histone protein deacetylation. In compartment-specific locations, candidate target proteins undergoing lysine-residue deacetylation are being identified. Through these investigations, the functional role of this post-translational modification is being delineated. We review the sirtuin family proteins, discuss their functional effects on target proteins, and postulate on potential biological programs and disease processes that may be modified by sirtuin-mediated deacetylation of target proteins.


SirtuinsLysine acetylation/deacetylationPost-translational modificationsNAD+Biological functions

Copyright information

© US Government 2010

Authors and Affiliations

  1. 1.Translational Medicine BranchNational Heart Lung and Blood Institute, NIHBethesdaUSA