title: Protein N-terminal acetyltransferases: when the start matters.
abstract: The majority of eukaryotic proteins are subjected to N-terminal acetylation (Nt-acetylation), catalysed by N-terminal acetyltransferases (NATs). Recently, the structure of an NAT-peptide complex was determined, and detailed proteome-wide Nt-acetylation patterns were revealed. Furthermore, Nt-acetylation just emerged as a multifunctional regulator, acting as a protein degradation signal, an inhibitor of endoplasmic reticulum (ER) translocation, and a mediator of protein complex formation. Nt-acetylation is regulated by acetyl-coenzyme A (Ac-CoA) levels, and thereby links metabolic cell states to cell death. The essentiality of NATs in humans is stressed by the recent discovery of a human hereditary lethal disease caused by a mutation in an NAT gene. Here, we discuss how these recent findings shed light on NATs as major protein regulators and key cellular players.
authors.affiliation: Department of Molecular Biology, University of Bergen, Bergen, Norway.
authors.forename: Kristian K
authors.initials: KK
authors.lastname: Starheim
authors.forename: Kris
authors.initials: K
authors.lastname: Gevaert
authors.forename: Thomas
authors.initials: T
authors.lastname: Arnesen
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D006801:Humans; D008954:Models, Biological; D011506:Proteins / Q000378:metabolism
chemical_list: D011506:Proteins; D000123:Acetyltransferases; C061313:protein N-terminal acetyltransferase