The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Proteomic Analysis of Lysine Acetylation Sites in Rat Tissues Reveals Organ Specificity and Subcellular Patterns
Open accessAbstract
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.
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Cites
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“Our approach relies on the label-free quantification measurements and uses the information contained in the normalized peptide intensities for a given acetylated peptide and its corresponding nonacetylated peptide combined with relative iBAQ estimated protein abundances between tissues (Schwanhäusser et al., 2011).”
MethodLysine acetylation targets protein complexes and co-regulates major cellular functions
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Cited by
Swatek, K. N., & Komander, D. (2016) · Cell Research · doi:10.1038/cr.2016.39 · Cited by 2,081
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Metadata
- Authors
- Lundby, A., Lage, K., Weinert, B. T., Bekker-Jensen, D. B., Secher, A., Skovgaard, T., Kelstrup, C. D., Dmytriyev, A., Choudhary, C., Lundby, C., & Olsen, J. V.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2012-08
- Volume
- 2
- Issue
- 2
- Pages
- 419-431
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2101065953
- Cited by
- 547
- References
- 15
- FWCI
- 19.69
- Type
- journal article
- Language
- en
- Open access
- gold
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