Nϵ-lysine acetylation in the lumen of the endoplasmic reticulum: A way to regulate autophagy and maintain protein homeostasis in the secretory pathway

Autophagy. 2016 Jun 2;12(6):1051-2. doi: 10.1080/15548627.2016.1164369. Epub 2016 Apr 28.

Abstract

The Nϵ-lysine acetylation of cargo proteins in the lumen of the endoplasmic reticulum (ER) requires a membrane transporter (SLC33A1) and 2 acetyltransferases (NAT8B and NAT8). The ER acetylation machinery regulates the homeostatic balance between quality control/efficiency of the secretory pathway and autophagy-mediated disposal of toxic protein aggregates. We recently reported that the autophagy pathway that acts downstream of the ER acetylation machinery specifically targets protein aggregates that form within the secretory pathway. Genetic and biochemical manipulation of ER acetylation in a mouse model of Alzheimer disease is able to restore normal proteostasis and rescue the disease phenotype. Here we summarize these findings and offer an overview of the ER-acetylation machinery.

Keywords: acetyl-CoA; autophagy; endoplasmic reticulum; lysine acetylation; secretory pathway.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, N.I.H., Extramural

MeSH terms

  • Acetylation
  • Animals
  • Autophagy*
  • Endoplasmic Reticulum / metabolism*
  • Homeostasis*
  • Humans
  • Models, Biological
  • Proteins / metabolism*
  • Secretory Pathway*

Substances

  • Proteins