TY - JOUR

T1 - Lysine acetylation in mitochondria

T2 - From inventory to function

AU - Hosp, Fabian

AU - Lassowskat, Ines

AU - Santoro, Valeria

AU - De Vleesschauwer, David

AU - Fliegner, Daniela

AU - Redestig, Henning

AU - Mann, Matthias

AU - Christian, Sven

AU - Hannah, Matthew A

AU - Finkemeier, Iris

N1 - Copyright © 2016 Elsevier B.V. and Mitochondria Research Society. All rights reserved.

PY - 2017/3

Y1 - 2017/3

N2 - 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.

AB - 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.

KW - Acetyl Coenzyme A

KW - Acetylation

KW - Animals

KW - Computational Biology

KW - Lysine

KW - Mass Spectrometry

KW - Mitochondria

KW - Mitochondrial Proteins

KW - Plants

KW - Protein Processing, Post-Translational

KW - Proteomics

KW - Journal Article

KW - Review

U2 - 10.1016/j.mito.2016.07.012

DO - 10.1016/j.mito.2016.07.012

M3 - Review

C2 - 27476757

VL - 33

SP - 58

EP - 71

JO - Mitochondrion

JF - Mitochondrion

SN - 1567-7249

ER -