Cited by 295Mitochondrial Function and PathologyMetabolism and Genetic DisordersBiochemical Acid Research Studies

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Mitochondrial Complex II: At the Crossroads

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Bezawork-Geleta, Ayenachew, Rohlena, Jakub, Dong, Lanfeng, Pacak, Karel, Neuzil, Jiri·2017·Trends in Biochemical Sciences

DOI 10.1016/j.tibs.2017.01.003PMC PMC7441821

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Abstract

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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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
Succinate Dehydrogenase Supports Metabolic Repurposing of Mitochondria to Drive Inflammatory Macrophages
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].”
Itaconate Links Inhibition of Succinate Dehydrogenase with Macrophage Metabolic Remodeling and Regulation of Inflammation
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
Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors
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
Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling
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].”

Show all 118 references

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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)
DOI: 10.1016/j.tibs.2017.01.003
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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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Mitochondrial Complex II: At the Crossroads

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