The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation
Open accessAbstract
Protein acetylation is a well-studied regulatory mechanism for several cellular processes, ranging from gene expression to metabolism. Recent discoveries of new post-translational modifications, including malonylation, succinylation, and glutarylation, have expanded our understanding of the types of modifications found on proteins. These three acidic lysine modifications are structurally similar but have the potential to regulate different proteins in different pathways. The deacylase sirtuin 5 (SIRT5) catalyzes the removal of these modifications from a wide range of proteins in different subcellular compartments. Here, we review these new modifications, their regulation by SIRT5, and their emerging role in cellular regulation and diseases.
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Cites
Lysine acetylation targets protein complexes and co-regulates major cellular functions
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Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
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Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
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Self-citationIdentification of lysine succinylation as a new post-translational modification
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Self-citationSIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
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Self-citationLysine glutarylation is a protein posttranslational modification regulated by SIRT5
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Sun, L., Zhang, H., & Gao, P. (2022) · Protein & Cell · doi:10.1007/s13238-021-00846-7 · Cited by 770
Metabolic Regulation of Gene Expression by Histone Lysine β-Hydroxybutyrylation
Xie, Z., Zhang, D., Chung, D., Tang, Z., Huang, H., Dai, L., Qi, S., Li, J., Colak, G., Chen, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.036 · Cited by 744
Self-citationKrebs cycle Reborn in macrophage immunometabolism
Ryan, D. G., & O'Neill, L. A. J. (2020) · Annual Review of Immunology · doi:10.1146/annurev-immunol-081619-104850 · Cited by 444
Wang, F., Wang, K., Xu, W., Zhao, S., Ye, D., Wang, Y., Xu, Y., Zhou, L., Chu, Y., Zhang, C., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.065 · Cited by 340
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Metadata
- Authors
- Hirschey, M. D., & Zhao, Y.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2015-09
- Volume
- 14
- Issue
- 9
- Pages
- 2308-2315
- ISSN
- 1535-9476 (ISSN-L)
- OpenAlex
- W2121046220
- Cited by
- 427
- References
- 18
- FWCI
- 18.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Hirschey, M. D., & Zhao, Y. (2015). Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation. Molecular & Cellular Proteomics. https://doi.org/10.1074/mcp.r114.046664
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