Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 37, Issue 4, Pages 152-161Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2012.02.003
Keywords
N-terminal acetylation; protein N-terminal acetyltransferase; Nt-proteomics; Ogden syndrome; NAA; protein degradation; endoplasmic reticulum translocation; acetyl-coenzyme A
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Funding
- Research Council of Norway [197136]
- Norwegian Cancer Society [171752- PR-2009-0222]
- Bergen Research Foundation (BFS)
- Fund for Scientific Research - Flanders (Belgium) [G.0042.07, G.0440.10]
- Inter University Attraction Poles [IUAP06]
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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.
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