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Mitochondrion. 2017 Mar;33:58-71. doi: 10.1016/j.mito.2016.07.012. Epub 2016 Jul 28.

Lysine acetylation in mitochondria: From inventory to function.

Author information

1
Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, DE-82152 Martinsried, Germany.
2
Plant Proteomics, Max Planck Institute for Plant Breeding Research, Carl von Linné Weg 10, DE-50829 Cologne, Germany.
3
Therapeutic Research Groups/Onc II, Bayer Pharma AG, Muellerstrasse 178, DE-13353 Berlin, Germany.
4
Bayer CropScience NV, Technologiepark 38, BL-9052 Gent (Zwijnaarde), Belgium.
5
Bayer Pharma AG, Department Heart and Lung Diseases Research, Aprather Weg 18a, DE-42113 Wuppertal, Germany.
6
Plant Proteomics, Max Planck Institute for Plant Breeding Research, Carl von Linné Weg 10, DE-50829 Cologne, Germany; Plant Physiology, Institute of Plant Biology and Biotechnology, University of Muenster, Schlossplatz 7, DE-48149 Muenster, Germany. Electronic address: iris.finkemeier@uni-muenster.de.

Abstract

Cellular signaling pathways are regulated in a highly dynamic fashion in order to quickly adapt to distinct environmental conditions. Acetylation of lysine residues represents a central process that orchestrates cellular metabolism and signaling. In mitochondria, acetylation seems to be the most prevalent post-translational modification, presumably linked to the compartmentation and high turnover of acetyl-CoA in this organelle. Similarly, the elevated pH and the higher concentration of metabolites in mitochondria seem to favor non-enzymatic lysine modifications, as well as other acylations. Hence, elucidating the mechanisms for metabolic control of protein acetylation is crucial for our understanding of cellular processes. Recent advances in mass spectrometry-based proteomics have considerably increased our knowledge of the regulatory scope of acetylation. Here, we review the current knowledge and functional impact of mitochondrial protein acetylation across species. We first cover the experimental approaches to identify and analyze lysine acetylation on a global scale, we then explore both commonalities and specific differences of plant and animal acetylomes and the evolutionary conservation of protein acetylation, as well as its particular impact on metabolism and diseases. Important future directions and technical challenges are discussed, and it is pointed out that the transfer of knowledge between species and diseases, both in technology and biology, is of particular importance for further advancements in this field.

KEYWORDS:

ATP synthase; Acetyl-CoA; Arabidopsis; Human; Lysine acetylation; Mitochondria; Mouse; Respiration; Rice; TCA cycle

PMID:
27476757
DOI:
10.1016/j.mito.2016.07.012
[Indexed for MEDLINE]

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