Control of Protein Degradation by N-terminal Acetylation and the N-end Rule Pathway

Exp Mol Med. 2018 Jul 27;50(7):1-8. doi: 10.1038/s12276-018-0097-y.

Abstract

Nα-terminal acetylation (Nt-acetylation) occurs very frequently and is found in most proteins in eukaryotes. Despite the pervasiveness and universality of Nt-acetylation, its general functions in terms of physiological outcomes remain largely elusive. However, several recent studies have revealed that Nt-acetylation has a significant impact on protein stability, activity, folding patterns, cellular localization, etc. In addition, Nt-acetylation marks specific proteins for degradation by a branch of the N-end rule pathway, a subset of the ubiquitin-mediated proteolytic system. The N-end rule associates a protein's in vivo half-life with its N-terminal residue or modifications on its N-terminus. This review provides a current understanding of intracellular proteolysis control by Nt-acetylation and the N-end rule pathway.

Publication types

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

MeSH terms

  • Acetylation
  • Animals
  • Humans
  • N-Terminal Acetyltransferases / metabolism*
  • Proteasome Endopeptidase Complex / metabolism
  • Proteolysis*
  • Ubiquitination*

Substances

  • N-Terminal Acetyltransferases
  • Proteasome Endopeptidase Complex