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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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Mei, X., He, X., Huang, L., Qi, D., Nie, J., Li, Y., Si, W., & Zhao, S. (2016) · FEBS Journal · doi:10.1111/febs.13912 · Cited by 12
Hseiky, A., Crespo, M., Kieffer‐Jaquinod, S., Fenaille, F., & Pflieger, D. (2021) · Proteomes · doi:10.3390/proteomes9020018 · Cited by 15
Li, J., Pan, H., Yang, H., Wang, C., Liu, H., Hui, Z., Li, P., Li, C., Lu, X., & Tian, Y. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.697963 · Cited by 12
Boradia, V. M., Patil, P., Agnihotri, A., Kumar, A., Rajwadi, K. K., Sahu, A., Bhagath, N., Sheokand, N., Kumar, M., Malhotra, H., et al. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0537-0 · Cited by 12
Succinylation – encoded metabolic codes: cracking the molecular logic of cellular adaptation
Cong, Y., Zhang, X., Wang, Z., Cui, Z., Li, C., Han, Y., Deng, W., Zhou, X., Wu, H., Sun, J., et al. (2025) · International Journal of Surgery · doi:10.1097/js9.0000000000003249 · Cited by 11
Crotonate enhances intestinal regeneration after injury via HBO1-mediated H3K14 crotonylation
Xiao, Y., Yu, S., Zhang, M., Zhong, N., Hua, S., Fang, Z. H., Zhang, Z., Liu, H., Tan, R., Liu, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63869-2 · Cited by 11
Self-citationSuccinate-driven PKM2 succinylation and dimerization accelerates age-associated cardiac fibrosis
Wang, Z., Zhang, Z., Ping, Z., Yang, S., Li, Y., Jiang, T., Zheng, X., Zhang, Q., Liu, Z., Zhang, X., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-09337-5 · Cited by 11
Self-citationZuo, Y., Hong, Y., Zeng, X., Zhang, Q., & Liu, X. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac277 · Cited by 11
Impact of Lysine Succinylation on the Biology of Fungi
Adejor, J., Tumukunde, E., Li, G., Lin, H., Xie, R., & Wang, S. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46020065 · Cited by 12
Yang, Y., Tan, L., He, S., Hao, B., Huang, X., Zhou, Y., Shang, W., Peng, H., Hu, Z., Ding, R., et al. (2024) · Microbiological Research · doi:10.1016/j.micres.2024.127635 · Cited by 11
Tran, T.-X., Le, N. Q. K., & Nguyen, V. (2025) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2025.109664 · Cited by 11
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
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