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Cell Rep. 2012 Aug 30;2(2):419-31. doi: 10.1016/j.celrep.2012.07.006. Epub 2012 Aug 16.

Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.

Author information

1
Novo Nordisk Foundation Center for Protein Research, Department for Proteomics, Faculty of Health Sciences, University of Copenhagen, Denmark.

Abstract

Lysine acetylation is a major posttranslational modification involved in a broad array of physiological functions. Here, we provide an organ-wide map of lysine acetylation sites from 16 rat tissues analyzed by high-resolution tandem mass spectrometry. We quantify 15,474 modification sites on 4,541 proteins and provide the data set as a web-based database. We demonstrate that lysine acetylation displays site-specific sequence motifs that diverge between cellular compartments, with a significant fraction of nuclear sites conforming to the consensus motifs G-AcK and AcK-P. Our data set reveals that the subcellular acetylation distribution is tissue-type dependent and that acetylation targets tissue-specific pathways involved in fundamental physiological processes. We compare lysine acetylation patterns for rat as well as human skeletal muscle biopsies and demonstrate its general involvement in muscle contraction. Furthermore, we illustrate that acetylation of fructose-bisphosphate aldolase and glycerol-3-phosphate dehydrogenase serves as a cellular mechanism to switch off enzymatic activity.

PMID:
22902405
PMCID:
PMC4103158
DOI:
10.1016/j.celrep.2012.07.006
[Indexed for MEDLINE]
Free PMC Article

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