Mitochondrial acetylation and genetic models of Parkinson's disease

Prog Mol Biol Transl Sci. 2014:127:155-82. doi: 10.1016/B978-0-12-394625-6.00006-4.

Abstract

Parkinson's disease (PD) is frequent at old age, leading to atrophy of specific neurons and to early death. Lifespan and healthy aging of organisms depend on growth factor/nutrient signaling and on bioenergetics via mitochondria, all of which regulate downstream nuclear functions through FOXO and SIR proteins. Mammalian SIRtuins include the mitochondrial deacetylase SIRT3, and recently mitochondrial lysine acetylation (AcLys) was found to initiate mitochondrial degradation by autophagy. This mitophagy process is closely regulated by PINK1 and Parkin, two interacting proteins which relocalize to mitochondria with deficient proton gradients, and whose mutations cause autosomal recessive variants of PD. Strong generalized deacetylation of mitochondrial proteins and altered SIRT3 levels occur in rodent models of PD before the onset of toxic aggregate formation. We propose that the development of site-specific AcLys-antibodies and their characterization in patients will have medical value.

Keywords: Alpha-Synuclein; Deacylases; Mitochondrial lysine acetylation; Mitophagy; PARKIN; PINK1; Parkinson's disease; Respiratory complex V; SIRT3.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Animals
  • Energy Metabolism
  • Humans
  • Mitochondria / metabolism*
  • Mitophagy
  • Models, Genetic*
  • Parkinson Disease / genetics*
  • Parkinson Disease / pathology*