Alpha‐ketoglutarate dehydrogenase complex‐dependent succinylation of proteins in neurons and neuronal cell lines
Open accessAbstract
Reversible post‐translation modifications of proteins are common in all cells and appear to regulate many processes. Nevertheless, the enzyme(s) responsible for the alterations and the significance of the modification are largely unknown. Succinylation of proteins occurs and causes large changes in the structure of proteins; however, the source of the succinyl groups, the targets, and the consequences of these modifications on other proteins remain unknown. These studies focused on succinylation of mitochondrial proteins. The results demonstrate that the α‐ketoglutarate dehydrogenase complex (KGDHC) can serve as a trans‐succinylase that mediates succinylation in an α‐ketoglutarate‐dependent manner. Inhibition of KGDHC reduced succinylation of both cytosolic and mitochondrial proteins in cultured neurons and in a neuronal cell line. Purified KGDHC can succinylate multiple proteins including other enzymes of the tricarboxylic acid cycle leading to modification of their activity. Inhibition of KGDHC also modifies acetylation by modifying the pyruvate dehydrogenase complex. The much greater effectiveness of KGDHC than succinyl‐CoA suggests that the catalysis owing to the E2k succinyltransferase is important. Succinylation appears to be a major signaling system and it can be mediated by KGDHC. image Reversible post‐translation modifications of proteins are common and may regulate many processes. Succinylation of proteins occurs and causes large changes in the structure of proteins. However, the source of the succinyl groups, the targets, and the consequences of these modifications on other proteins remains unknown. The results demonstrate that the mitochondrial α‐ketoglutarate dehydrogenase complex (KGDHC) can succinylate multiple mitochondrial proteins and alter their function. Succinylation appears to be a major signaling system and it can be mediated by KGDHC.
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Citrate acts as a source of acetyl-CoA to drive histone acetylation, with impacts on tumor and immune cell function.
“Citrate, a component of the TCA cycle has been shown to act as a source of acetyl-CoA to drive histone acetylation and this process can have profound impacts on both tumor and immune cell function.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [53]
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- Authors
- Gibson, G. E., Xu, H., Chen, H., Chen, W., Denton, T. T., & Zhang, S.
- Affiliations
- Burke Medical Research Institute (US)
- Cornell University (US)
- Washington State University Spokane (US)
- Corresponding author
- Gibson, Gary E.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2015-04-08
- Volume
- 134
- Issue
- 1
- Pages
- 86-96
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- PMC
- PMC4472501
- OpenAlex
- W1973148168
- Cited by
- 137
- References
- 30
- Citations by year
- 2026: 8 · 2025: 18 · 2024: 17 · 2023: 10 · 2022: 11 · 2021: 22 · 2020: 12 · 2019: 9 · 2018: 7 · 2017: 11 · 2016: 7 · 2015: 5
- FWCI
- 4.94
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH (AG14930, 1S10RR025449-01)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- succinylation, alpha-ketoglutarate dehydrogenase complex, post-translational modification, mitochondrial proteins, neurons, neuronal cell lines, pyruvate dehydrogenase complex, acetylation, tricarboxylic acid cycle enzymes, succinyl-CoA
- MeSH terms
- Acyl Coenzyme A, Animals, Brain, Cell Line, Cells, Cultured, Female, Ketoglutarate Dehydrogenase Complex, Male, Mice, Inbred C57BL, Nerve Tissue Proteins, Neurons, Sirtuins, Mice
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