Mechanisms and Dynamics of Protein Acetylation in Mitochondria.

Josue Baeza, Michael J Smallegan, John M Denu

Journal: Trends in biochemical sciences 2016;41(3):231-244

PMID: 26822488

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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.

Address: Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53715, USA; Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI 53715, USA.; Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI 53715, USA.; Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53715, USA; Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI 53715, USA. Electronic address: [email protected].

DOI: 10.1016/j.tibs.2015.12.006