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Cell Rep DOI:10.1016/j.celrep.2012.07.006

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

Publication TypeJournal Article
Year of Publication2012
AuthorsLundby, A, Lage, K, Weinert, BT, Bekker-Jensen, DB, Secher, A, Skovgaard, T, Kelstrup, CD, Dmytriyev, A, Choudhary, C, Lundby, C, Olsen, JV
JournalCell Rep
Date Published2012 Aug 30
KeywordsAcetylation, Amino Acid Motifs, Animals, Humans, Lysine, Organ Specificity, Protein Processing, Post-Translational, Proteome, Proteomics, Rats, Rats, Sprague-Dawley

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.


Alternate JournalCell Rep
PubMed ID22902405
PubMed Central IDPMC4103158
Grant ListP01 HD068250 / HD / NICHD NIH HHS / United States