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Identification of lysine succinylation as a new post-translational modification
Open accessAbstract
Of the 20 ribosomally coded amino acid residues, lysine is the most frequently post-translationally modified, which has important functional and regulatory consequences. Here we report the identification and verification of a previously unreported form of protein post-translational modification (PTM): lysine succinylation. The succinyllysine residue was initially identified by mass spectrometry and protein sequence alignment. The identified succinyllysine peptides derived from in vivo proteins were verified by western blot analysis, in vivo labeling with isotopic succinate, MS/MS and HPLC coelution of their synthetic counterparts. We further show that lysine succinylation is evolutionarily conserved and that this PTM responds to different physiological conditions. Our study also implies that succinyl-CoA might be a cofactor for lysine succinylation. Given the apparent high abundance of lysine succinylation and the significant structural changes induced by this PTM, it is expected that lysine succinylation has important cellular functions.
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In the citing paper
“recent studies have revealed novel roles for sirt4 and sirt5 in regulating protein malonylation and succinylation (Du et al., 2011; Peng et al., 2011; Zhang et al., 2011)”
From Lipid-Induced Mitochondrial Stress and Insulin Action in Muscle (2012) · cites this paper as Zhang et al., 2011
In the citing paper
“The mitochondrial sirtuin SIRT5 removes malonyl and succinyl moieties from target lysines.”
From SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways (2013) · cites this paper as Zhang et al., 2011
In the citing paper
“Recently, we identified and fully validated Lys succinylation and malonylation as PTM pathways, implying an ancient conserved function (Peng et al., 2011; Zhang et al., 2011).”
From SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways (2013) · cites this paper as Zhang et al., 2011
In the citing paper
“Our work, as well as that of others, has identified SIRT5 as the only known enzyme to date catalyzing Lys desuccinylation and demalonylation (Du et al., 2011; Peng et al., 2011; Zhang et al., 2011).”
From SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways (2013) · cites this paper as Zhang et al., 2011
In the citing paper
“Our previous studies identified Ksucc sites on E. coli IDH (Zhang et al., 2011).”
From SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways (2013) · cites this paper as Zhang et al., 2011
In the citing paper
“The authors demonstrate that SIRT5 desuccinylates and activates PKM2 and this limits IL-1β production.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [46]
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Metadata
- Authors
- Zhang, Z., Tan, M., Xie, Z., Dai, L., Chen, Y., & Zhao, Y.
- Affiliations
- University of Chicago (US)
- Corresponding author
- Zhao, Yingming
- Venue
- Nature Chemical Biology
- Published
- 2010-12-12
- Volume
- 7
- Issue
- 1
- Pages
- 58-63
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- PMC
- PMC3065206
- OpenAlex
- W1969899640
- Cited by
- 1,027
- References
- 23
- Citations by year
- 2026: 99 · 2025: 114 · 2024: 102 · 2023: 83 · 2022: 100 · 2021: 95 · 2020: 60 · 2019: 49 · 2018: 64 · 2017: 45 · 2016: 57 · 2015: 48 · 2014: 36 · 2013: 33 · 2012: 25
- FWCI
- 10.57
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01CA126832)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- lysine succinylation, post-translational modification, succinyl-CoA, protein modification, evolutionary conservation, protein structure-function relationship
- MeSH terms
- Acyl Coenzyme A, Amino Acid Sequence, Chromatography, High Pressure Liquid, Lysine, Molecular Sequence Data, Peptides, Protein Processing, Post-Translational, Mass Spectrometry, Blotting, Western, Sequence Alignment, Succinic Acid, Escherichia coli Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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