Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases

Recent studies of N-terminal acetylation have identified new N-terminal acetyltransferases (NATs) and expanded the known functions of these enzymes beyond their roles as ribosome-associated co-translational modifiers. For instance, the identification of Golgi- and chloroplast-associated NATs shows t...

Full description

Saved in:
Bibliographic Details
Published in:Molecular cell 2019-03, Vol.73 (6), p.1097-1114
Main Authors: Aksnes, Henriette, Ree, Rasmus, Arnesen, Thomas
Format: Article
Language:English
Subjects:
Acetylation
actin
Animals
Catalysis
Humans
KAT
lysine acetyltransferase
N-terminal acetylation
N-terminal acetyltransferase
N-Terminal Acetyltransferases - metabolism
NAA10
NAA80
NAT
Proteasome Endopeptidase Complex - metabolism
Protein Domains
protein modifications
Protein Processing, Post-Translational
Proteolysis
Signal Transduction
Substrate Specificity
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Recent studies of N-terminal acetylation have identified new N-terminal acetyltransferases (NATs) and expanded the known functions of these enzymes beyond their roles as ribosome-associated co-translational modifiers. For instance, the identification of Golgi- and chloroplast-associated NATs shows that acetylation of N termini also happens post-translationally. In addition, we now appreciate that some NATs are highly specific; for example, a dedicated NAT responsible for post-translational N-terminal acetylation of actin was recently revealed. Other studies have extended NAT function beyond Nt acetylation, including functions as lysine acetyltransferases (KATs) and non-catalytic roles. Finally, emerging studies emphasize the physiological relevance of N-terminal acetylation, including roles in calorie-restriction-induced longevity and pathological α-synuclein aggregation in Parkinson’s disease. Combined, the NATs rise as multifunctional proteins, and N-terminal acetylation is gaining recognition as a major cellular regulator. N-terminal acetylation, long considered a co-translational and static modification, recently stepped into the post-translational world, and several reports now suggest regulation and crosstalk with other modifications as well as moonlighting functions. Aksnes et al. review novel functions of N-terminal acetyltransferases, including the most recently described Nt acetylation of actin.
ISSN:1097-2765
1097-4164
DOI:10.1016/j.molcel.2019.02.007