Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 41, Issue 3, Pages 231-244Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2015.12.006
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Funding
- National Institutes of Health (NIH) [GM065386]
- NIH National Research Service Award [T32 GM007215]
- National Science Foundation Graduate Research Fellowship Program (NSF-GRFP) [DGE-1256259]
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Reversible protein acetylation is a major regulatory mechanism for controlling protein function. Through genetic manipulations, dietary perturbations, and new proteomic technologies, the diverse functions of protein acetylation are coming into focus. Protein acetylation in mitochondria has taken center stage, revealing that 63% of mitochondrially localized proteins contain lysine acetylation sites. We summarize the field and discuss salient topics that cover spurious versus targeted acetylation, the role of SIRT3 deacetylation, nonenzymatic acetylation, and molecular models for regulatory acetylations that display high and low stoichiometry.
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