The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation
Open accessAbstract
The protein substrates of sirtuin 5-regulated lysine malonylation (Kmal) remain unknown, hindering its functional analysis. In this study, we carried out proteomic screening, which identified 4042 Kmal sites on 1426 proteins in mouse liver and 4943 Kmal sites on 1822 proteins in human fibroblasts. Increased malonyl-CoA levels in malonyl-CoA decarboxylase (MCD)-deficient cells induces Kmal levels in substrate proteins. We identified 461 Kmal sites showing more than a 2-fold increase in response to MCD deficiency as well as 1452 Kmal sites detected only in MCD-/- fibroblast but not MCD+/+ cells, suggesting a pathogenic role of Kmal in MCD deficiency. Cells with increased lysine malonylation displayed impaired mitochondrial function and fatty acid oxidation, suggesting that lysine malonylation plays a role in pathophysiology of malonic aciduria. Our study establishes an association between Kmal and a genetic disease and offers a rich resource for elucidating the contribution of the Kmal pathway and malonyl-CoA to cellular physiology and human diseases.
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Cites
Lysine acetylation targets protein complexes and co-regulates major cellular functions
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Self-citationSirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
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Self-citationSIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
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BackgroundResultSelf-citationSIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
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Impairment of Angiogenesis by Fatty Acid Synthase Inhibition Involves mTOR Malonylation
Bruning, U., Morales-Rodriguez, F., Kalucka, J., Goveia, J., Taverna, F., Queiroz, K. C. S., Dubois, C., Cantelmo, A. R., Chen, R., Loroch, S., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.07.019 · Cited by 282
Compartmentalised acyl-CoA metabolism and roles in chromatin regulation
Trefely, S., Lovell, C. D., Snyder, N. W., & Wellen, K. E. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.01.005 · Cited by 272
Beyond repression of Nrf2: An update on Keap1
Kopacz, A., Kloska, D., Forman, H. J., Jozkowicz, A., & Grochot-Przeczek, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.023 · Cited by 265
Metadata
- Authors
- Colak, G., Pougovkina, O., Dai, L., Tan, M., te Brinke, H., Huang, H., Cheng, Z., Park, J., Wan, X., Liu, X., Yue, W. W., Wanders, R. J. A., Locasale, J. W., Lombard, D. B., de Boer, V. C. J., & Zhao, Y.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 14
- Issue
- 11
- Pages
- 3056-3071
- ISSN
- 1535-9476 (ISSN-L)
- OpenAlex
- W2119861196
- Cited by
- 190
- References
- 15
- FWCI
- 11.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Colak, G., Pougovkina, O., Dai, L., Tan, M., te Brinke, H., Huang, H., Cheng, Z., Park, J., Wan, X., Liu, X., Yue, W. W., Wanders, R. J. A., Locasale, J. W., Lombard, D. B., de Boer, V. C. J., & Zhao, Y. (2015). Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. Molecular & Cellular Proteomics. https://doi.org/10.1074/mcp.m115.048850
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