The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Lysine Succinylation Is a Frequently Occurring Modification in Prokaryotes and Eukaryotes and Extensively Overlaps with Acetylation
Open accessAbstract
Recent studies have shown that lysines can be posttranslationally modified by various types of acylations. However, except for acetylation, very little is known about their scope and cellular distribution. We mapped thousands of succinylation sites in bacteria (E. coli), yeast (S. cerevisiae), human (HeLa) cells, and mouse liver tissue, demonstrating widespread succinylation in diverse organisms. A majority of succinylation sites in bacteria, yeast, and mouse liver were acetylated at the same position. Quantitative analysis of succinylation in yeast showed that succinylation was globally altered by growth conditions and mutations that affected succinyl-coenzyme A (succinyl-CoA) metabolism in the tricarboxylic acid cycle, indicating that succinylation levels are globally affected by succinyl-CoA concentration. We preferentially detected succinylation on abundant proteins, suggesting that succinylation occurs at a low level and that many succinylation sites remain unidentified. These data provide a systems-wide view of succinylation and its dynamic regulation and show its extensive overlap with acetylation.
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Cites
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“Succinylation Abundance In order to determine the relationship between protein abundance and succinylation in our samples, we determined relative protein abundances using an intensity-based absolute quantification (iBAQ) method (Schwanhäusser et al., 2011).”
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Global analysis of protein expression in yeast
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ATP-citrate lyase links cellular metabolism to histone acetylation
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Regulation of cellular metabolism by protein lysine acetylation
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Cited by
Metabolic reprogramming in macrophages and dendritic cells in innate immunity
Kelly, B., & O'Neill, L. A. (2015) · Cell Research · doi:10.1038/cr.2015.68 · Cited by 1,876
The growing landscape of lysine acetylation links metabolism and cell signalling
Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324
Self-citationFunctions and mechanisms of non-histone protein acetylation
Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232
Self-citationLysine glutarylation is a protein posttranslational modification regulated by SIRT5
Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.014 · Cited by 844
“In addition, lysine succinylation is an abundant protein PTM in diverse model organisms (Weinert et al., 2013).”
Backgroundβ-Hydroxybutyrate: A Signaling Metabolite
Newman, J. C., & Verdin, E. (2017) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064916 · Cited by 872
Metadata
- Authors
- Weinert, B. T., Schölz, C., Wagner, S. A., Iesmantavicius, V., Su, D., Daniel, J. A., & Choudhary, C.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2013-08
- Volume
- 4
- Issue
- 4
- Pages
- 842-851
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2114836779
- Cited by
- 753
- References
- 29
- FWCI
- 19.84
- Type
- journal article
- Language
- en
- Open access
- gold
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- Weinert, B. T., Schölz, C., Wagner, S. A., Iesmantavicius, V., Su, D., Daniel, J. A., & Choudhary, C. (2013). Lysine Succinylation Is a Frequently Occurring Modification in Prokaryotes and Eukaryotes and Extensively Overlaps with Acetylation. Cell Reports. https://doi.org/10.1016/j.celrep.2013.07.024
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