| Literature DB >> 26822488 |
Josue Baeza1, Michael J Smallegan2, John M Denu3.
Abstract
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.Entities:
Keywords: acetylation; acylation; metabolic regulation; mitochondria; nonenzymatic; stoichiometry
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Year: 2016 PMID: 26822488 PMCID: PMC4783225 DOI: 10.1016/j.tibs.2015.12.006
Source DB: PubMed Journal: Trends Biochem Sci ISSN: 0968-0004 Impact factor: 13.807