Protein N-terminal acetyltransferases: when the start matters

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• 作者：Kristian K. Starheim¹ ; ² ; Kris Gevaert³ ; ⁴ ; Thomas Arnesen¹ ; ⁵ ; ^{thomas.arnesen@mbi.uib.no}
• 关键词：N-terminal acetylation ; protein N-terminal acetyltransferase ; Nt-proteomics ; Ogden syndrome ; NAA ; protein degradation ; endoplasmic reticulum translocation ; acetyl-coenzyme A
• 刊名：Trends in Biochemical Sciences
• 出版年：2012
• 出版时间：April, 2012
• 年：2012
• 卷：37
• 期：4
• 页码：152-161
• 全文大小：1187 K

文摘

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.