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

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 dona...

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Bibliographic Details
Published in:Cellular and molecular life sciences : CMLS 2010-09, Vol.67 (18), p.3073-3087
Main Authors: Bao, Jianjun, Sack, Michael N
Format: Article
Language:English
Subjects:
Acetylation
Amino acids
Biochemistry
Biological functions
Biomedical and Life Sciences
Biomedicine
Cell Biology
Cellular biology
Humans
Life Sciences
Lysine acetylation/deacetylation
Mitochondria - enzymology
Molecular biology
NAD
Neoplasms - enzymology
Neurons - enzymology
Nutrient availability
Nutrient status
Oxidation-Reduction
Phylogeny
Post-translational modifications
Protein Processing, Post-Translational
Protein synthesis
Proteins
Proteins - metabolism
Review
Sirtuins
Sirtuins - classification
Sirtuins - metabolism
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Summary: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.
ISSN:1420-682X
1420-9071
DOI:10.1007/s00018-010-0402-y