Mitochondrial protein acetylation regulates metabolism.

Journal Article (Review)

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.

Full Text

Duke Authors

Cited Authors

  • Anderson, KA; Hirschey, MD

Published Date

  • 2012

Published In

Volume / Issue

  • 52 /

Start / End Page

  • 23 - 35

PubMed ID

  • 22708561

Electronic International Standard Serial Number (EISSN)

  • 1744-1358

Digital Object Identifier (DOI)

  • 10.1042/bse0520023

Language

  • eng

Conference Location

  • England