The DOI matches its Crossref record; 118 of the 118 references it cites were found in a registry or an index.
Mitochondrial Complex II: At the Crossroads
Open accessAbstract
Mitochondrial complex II (CII), also called succinate dehydrogenase (SDH), is a central purveyor of the reprogramming of metabolic and respiratory adaptation in response to various intrinsic and extrinsic stimuli and abnormalities. In this review we discuss recent findings regarding SDH biogenesis, which requires four known assembly factors, and modulation of its enzymatic activity by acetylation, succinylation, phosphorylation, and proteolysis. We further focus on the emerging role of both genetic and epigenetic aberrations leading to SDH dysfunction associated with various clinical manifestations. This review also covers the recent discovery of the role of SDH in inflammation-linked pathologies. Conceivably, SDH is a potential target for several hard-to-treat conditions, including cancer, that remains to be fully exploited.
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“Complex II is also capable of matrix mtROS production [100,101,102,103,104] and two different modes of production were described:”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [101]
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Cites
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS
Chouchani, E. T., Pell, V. R., Gaude, E., Aksentijević, D., Sundier, S. Y., Robb, E. L., Logan, A., Nadtochiy, S. M., Ord, E. N. J., Smith, A. C., et al. (2014) · Nature · doi:10.1038/nature13909 · Cited by 2,907
Mills, E. L., Kelly, B., Logan, A., Costa, A. S. H., Varma, M., Bryant, C. E., Tourlomousis, P., Däbritz, J. H. M., Gottlieb, E., Latorre, I., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.064 · Cited by 2,291
Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-α prolyl hydroxylase
Selak, M. A., Armour, S. M., MacKenzie, E. D., Boulahbel, H., Watson, D. G., Mansfield, K. D., Pan, Y., Simon, M. C., Thompson, C. B., & Gottlieb, E. (2005) · Cancer Cell · doi:10.1016/j.ccr.2004.11.022 · Cited by 2,108 · cited 1×
“Succinate has also been shown to inhibit another dioxygenase family of proteins, the prolyl 4-hydroxylases-2 and -3, that posttranslationally regulate Hif1a by its stabilization [12,23].”
Lampropoulou, V., Sergushichev, A., Bambousková, M., Nair, S., Vincent, E. E., Loginicheva, E., Cervantes‐Barragán, L., Ma, X., Huang, S. C., Griss, T., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.004 · Cited by 1,583
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487
Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
Xiao, M., Yang, H., Xu, W., Ma, S., Lin, H., Zhu, H., Liu, L., Liu, Y., Yang, C., Xu, Y., et al. (2012) · Genes & Development · doi:10.1101/gad.191056.112 · Cited by 1,188
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063
Role of TET enzymes in DNA methylation, development, and cancer
Rasmussen, K. D., & Helin, K. (2016) · Genes & Development · doi:10.1101/gad.276568.115 · Cited by 1,040 · cited 2×
“It has been shown that succinate inhibits the enzymatic activity of TET proteins and leads to the loss of 5hmC [85,89].”
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Domínguez‐Andrés, J., Novakovic, B., Li, Y., Scicluna, B. P., Gresnigt, M. S., Arts, R. J. W., Oosting, M., Moorlag, S. J. C. F. M., Groh, L. A., Zwaag, J., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.09.003 · Cited by 403
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Metadata
- Authors
- Bezawork-Geleta, A., Rohlena, J., Dong, L., Pacak, K., & Neuzil, J.
- Affiliations
- Czech Academy of Sciences (CZ)
- ORCID
- Rohlena, Jakub
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2017-04
- Volume
- 42
- Issue
- 4
- Pages
- 312-325
- ISSN
- 0968-0004 (ISSN-L)
- PMC
- PMC7441821
- OpenAlex
- W2586320694
- Cited by
- 295
- References
- 118
- Citations by year
- 2026: 30 · 2025: 36 · 2024: 35 · 2023: 36 · 2022: 30 · 2021: 45 · 2020: 31 · 2019: 29 · 2018: 17 · 2017: 5
- FWCI
- 2.10
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- ASEP (submittedVersion, public-domain)
- Griffith Research Online (submittedVersion)
- Funders
- Australian Research Council (15-02203S)
- Czech Science Foundation (16-12719S, 17-20904S)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Keywords
- succinate dehydrogenase, assembly factors, post-translational modification, acetylation, succinylation, phosphorylation, proteolysis, epigenetic aberrations, inflammation, cancer, metabolic reprogramming, respiratory adaptation
- MeSH terms
- Animals, Humans, Inflammation, Mitochondria, Succinate Dehydrogenase
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