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Mechanisms and Dynamics of Protein Acetylation in Mitochondria.
Baeza, Josue; Smallegan, Michael J; Denu, John M.
Afiliação
  • Baeza J; Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53715, USA; Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI 53715, USA.
  • Smallegan MJ; Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI 53715, USA.
  • Denu JM; 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: john.denu@wisc.edu.
Trends Biochem Sci ; 41(3): 231-244, 2016 Mar.
Article em En | MEDLINE | ID: mdl-26822488
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas / Mitocôndrias Idioma: En Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas / Mitocôndrias Idioma: En Ano de publicação: 2016 Tipo de documento: Article