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Biochim Biophys Acta. 2016 Oct;1864(10):1372-401. doi: 10.1016/j.bbapap.2016.06.007. Epub 2016 Jun 11.

The world of protein acetylation.

Author information

1
Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
2
Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway; Department of Surgery, Haukeland University Hospital, N-5021 Bergen, Norway.
3
Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway; Department of Surgery, Haukeland University Hospital, N-5021 Bergen, Norway. Electronic address: Thomas.Arnesen@uib.no.

Abstract

Acetylation is one of the major post-translational protein modifications in the cell, with manifold effects on the protein level as well as on the metabolome level. The acetyl group, donated by the metabolite acetyl-coenzyme A, can be co- or post-translationally attached to either the α-amino group of the N-terminus of proteins or to the ε-amino group of lysine residues. These reactions are catalyzed by various N-terminal and lysine acetyltransferases. In case of lysine acetylation, the reaction is enzymatically reversible via tightly regulated and metabolism-dependent mechanisms. The interplay between acetylation and deacetylation is crucial for many important cellular processes. In recent years, our understanding of protein acetylation has increased significantly by global proteomics analyses and in depth functional studies. This review gives a general overview of protein acetylation and the respective acetyltransferases, and focuses on the regulation of metabolic processes and physiological consequences that come along with protein acetylation.

KEYWORDS:

HAT; KAT; N-terminal acetylation; NAT; Post-translational modification; acetyltransferase; deacetylation; lysine acetylation

PMID:
27296530
DOI:
10.1016/j.bbapap.2016.06.007
[Indexed for MEDLINE]
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