title: First Things First: Vital Protein Marks by N-Terminal Acetyltransferases.
abstract: N-terminal (Nt) acetylation is known to be a highly abundant co-translational protein modification, but the recent discovery of Golgi- and chloroplast-resident N-terminal acetyltransferases (NATs) revealed that it can also be added post-translationally. Nt-acetylation may act as a degradation signal in a novel branch of the N-end rule pathway, whose functions include the regulation of human blood pressure. Nt-acetylation also modulates protein interactions, targeting, and folding. In plants, Nt-acetylation plays a role in the control of resistance to drought and in regulation of immune responses. Mutations of specific human NATs that decrease their activity can cause either the lethal Ogden syndrome or severe intellectual disability and cardiovascular defects. In sum, recent advances highlight Nt-acetylation as a key factor in many biological pathways.
authors: Department of Molecular Biology, University of Bergen, 5020 Bergen, Norway.
authors: Henriette
authors: H
authors: Aksnes
authors: Department of Molecular Biology, University of Bergen, 5020 Bergen, Norway.
authors: Adrian
authors: A
authors: Drazic
authors: Department of Molecular Biology, University of Bergen, 5020 Bergen, Norway.
authors: Michaël
authors: M
authors: Marie
authors: Department of Molecular Biology, University of Bergen, 5020 Bergen, Norway; Department of Surgery, Haukeland University Hospital, 5021 Bergen, Norway. Electronic address: thomas.arnesen@uib.no.
authors: Thomas
authors: T
authors: Arnesen
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009154:Mutation; D011499:Protein Processing, Post-Translational
chemical_list: D000123:Acetyltransferases
keywords: N-terminal acetylation; N-terminal acetyltransferase (NAT); Nα-acetyltransferase (Naa); protein folding; protein interactions; protein stability.