Mitochondrial protein acetylation regulates metabolism.
Changes in cellular nutrient availability or energy status induce global changes in mitochondrial protein acetylation. Over one-third of all proteins in the mitochondria are acetylated, of which the majority are involved in some aspect of energy metabolism. Mitochondrial protein acetylation is regulated by SIRT3 (sirtuin 3), a member of the sirtuin family of NAD+-dependent protein deacetylases that has recently been identified as a key modulator of energy homoeostasis. In the absence of SIRT3, mitochondrial proteins become hyperacetylated, have altered function, and contribute to mitochondrial dysfunction. This chapter presents a review of the functional impact of mitochondrial protein acetylation, and its regulation by SIRT3.
Duke University Medical Center, Durham, NC 27704, U.S.A.
Kristin A
KA
Anderson
Matthew D
MD
Hirschey
D000107:Acetylation; D000818:Animals; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*; D024101:Mitochondrial Proteins / Q000378:metabolism*; D008954:Models, Biological; D056566:Sirtuin 3 / Q000378:metabolism
D024101:Mitochondrial Proteins; D056566:Sirtuin 3