Mitochondrial complex ii: At the crossroads

Bezawork-Geleta, Ayenachew; Rohlena, Jakub; Dong, Lanfeng; Pacak, Karel; Neuzil, Jiri

doi:10.1016/j.tibs.2017.01.003

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

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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Complex II is capable of matrix mtROS production.
“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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Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells
Cervera, A. M., Bayley, J.-P., Devilee, P., & McCreath, K. J. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-89 · Cited by 156 · see citing works
Potential functional roles of DNA demethylation intermediates
Song, C.-X., & He, C. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.07.003 · Cited by 154 · see citing works
Post-translational modifications in mitochondria: protein signaling in the powerhouse
Stram, A. R., & Payne, R. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2280-4 · Cited by 149 · see citing works
Dual Function of Sdh3 in the Respiratory Chain and TIM22 Protein Translocase of the Mitochondrial Inner Membrane
Gebert, N., Gebert, M., Oeljeklaus, S., von der Malsburg, K., Stroud, D. A., Kulawiak, B., Wirth, C., Zahedi, R. P., Doležal, P., Wiese, S., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.025 · Cited by 145 · see citing works
Recurrent Mutations of Chromatin-Remodeling Genes and Kinase Receptors in Pheochromocytomas and Paragangliomas
Toledo, R. A., Qin, Y., Cheng, Z.-M., Gao, Q., Iwata, S., Silva, G. M., Prasad, M. L., Ocal, I. T., Rao, S. N., D, N. A. M., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1841 · Cited by 139 · see citing works
Q-site inhibitor induced ROS production of mitochondrial complex II is attenuated by TCA cycle dicarboxylates
Siebels, I., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.06.005 · Cited by 130 · see citing works
Suppression of Tumor GrowthIn vivoby the Mitocan α-tocopheryl Succinate Requires Respiratory Complex II
Dong, L., Freeman, R., Liu, J., Zobalová, R., Marín‐Hernández, Á., Stantic, M., Rohlena, J., Vališ, K., Rodríguez‐Enríquez, S., Butcher, B., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2439 · Cited by 125 · see citing works
Self-citation
Protein-mediated assembly of succinate dehydrogenase and its cofactors
Vranken, J. G. V., Na, U., Winge, D. R., & Rutter, J. P. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2014.990556 · Cited by 122 · see citing works
ROS-Triggered Phosphorylation of Complex II by Fgr Kinase Regulates Cellular Adaptation to Fuel Use
Acín‐Pérez, R., Carrascoso, I., Baixauli, F., Roche-Molina, M., Latorre, A., Fernández‐Silva, P., Mittelbrunn, M., Sánchez‐Madrid, F., Martos, A. P., Lowell, C. A., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.015 · Cited by 120 · see citing works
Disease-Causing SDHAF1 Mutations Impair Transfer of Fe-S Clusters to SDHB
Maio, N., Ghezzi, D., Verrigni, D., Rizza, T., Bertini, E., Martinelli, D., Zeviani, M., Singh, A., Carrozzo, R., & Rouault, T. A. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.12.005 · Cited by 115 · see citing works
The LYR Factors SDHAF1 and SDHAF3 Mediate Maturation of the Iron-Sulfur Subunit of Succinate Dehydrogenase
Na, U., Yu, W., Cox, J. E., Bricker, D. K., Brockmann, K., Rutter, J. P., Thummel, C. S., & Winge, D. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.05.014 · Cited by 114 · see citing works
SDHAF4 Promotes Mitochondrial Succinate Dehydrogenase Activity and Prevents Neurodegeneration
Vranken, J. G. V., Bricker, D. K., Dephoure, N., Gygi, S. P., Cox, J. E., Thummel, C. S., & Rutter, J. P. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.05.012 · Cited by 108 · see citing works
Renal Tumors and Hereditary Pheochromocytoma-Paraganglioma Syndrome Type 4
Gill, A. J., Pachter, N., Clarkson, A., Tucker, K., Winship, I., Benn, D. E., Robinson, B. G., & Clifton-Bligh, R. J. (2011) · New England Journal of Medicine · doi:10.1056/nejmc1012357 · Cited by 106 · see citing works
SDH-related pheochromocytoma and paraganglioma
Kantorovich, V., King, K. S., & Pacák, K. (2010) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2010.04.001 · Cited by 105 · see citing works
Mitochondrial complex II, a novel target for anti-cancer agents
Kluckova, K., Bezawork-Geleta, A., Rohlena, J., Dong, L., & Neuzil, J. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.10.015 · Cited by 104 · see citing works
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Anticancer Drugs Targeting the Mitochondrial Electron Transport Chain
Rohlena, J., Dong, L.-F., Ralph, S. J., & Neuzil, J. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3990 · Cited by 91 · see citing works
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A PTEN-like Phosphatase with a Novel Substrate Specificity
Pagliarini, D. J., Worby, C. A., & Dixon, J. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404959200 · Cited by 85 · see citing works
Succinate: A New Epigenetic Hacker
Yang, M. H., & Pollard, P. J. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.05.015 · Cited by 84 · see citing works
Homozygous Gly555Glu mutation in the nuclear‐encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II
Coster, R. V., Seneca, S., Smet, J., Hecke, R. V., Gerlo, E., Devreese, B. V., BEEUMEN, J. V., Leroy, J. G., Meırleır, L. D., & Lissens, W. (2003) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.10202 · Cited by 83 · see citing works
Respiratory chain complex II as general sensor for apoptosis
Grimm, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.09.009 · Cited by 82 · see citing works
Succinate Dehydrogenase (SDH)-Deficient Pancreatic Neuroendocrine Tumor Expands the SDH-Related Tumor Spectrum
Niemeijer, N. D., Papathomas, T. G., Korpershoek, E., de Krijger, R. R., Oudijk, L., Morreau, H., Bayley, J., Hes, F. J., Jansen, J. C., Dinjens, W. N. M., et al. (2015) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-2689 · Cited by 81 · see citing works
Succinate dehydrogenase assembly factor 2 is needed for assembly and activity of mitochondrial complex II and for normal root elongation in A rabidopsis
Huang, S., Taylor, N. L., Ströher, E., Fenske, R., & Millar, A. H. (2012) · The Plant Journal · doi:10.1111/tpj.12041 · Cited by 75 · see citing works
The Tumor Suppressor cybL, a Component of the Respiratory Chain, Mediates Apoptosis Induction
Albayrak, T., Scherhammer, V., Schoenfeld, N., Braziulis, E., Mund, T., Bauer, M. K. A., Scheffler, I. E., & Grimm, S. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-10-0631 · Cited by 75 · see citing works
Carney triad can be (rarely) associated with germline succinate dehydrogenase defects
Boikos, S. A., Xekouki, P., Fumagalli, E. R., Faucz, F. R., Raygada, M. J., Szarek, E., Ball, E. R., Kim, S., Miettinen, M., Helman, L. J., et al. (2015) · European Journal of Human Genetics · doi:10.1038/ejhg.2015.142 · Cited by 68 · see citing works
Ubiquinone-binding site mutagenesis reveals the role of mitochondrial complex II in cell death initiation
Kluckova, K., Sticha, M., Cerny, J., Mracek, T., Dong, L., Drahota, Z., Gottlieb, E., Neuzil, J., & Rohlena, J. (2015) · Cell Death & Disease · doi:10.1038/cddis.2015.110 · Cited by 66 · cited 4× · see citing works
“We have also shown that CII mutations that significantly reduce CII activity and therefore elevate intracellular succinate suppress CII-derived ROS [72].”
InfluentialSelf-citation
Morphologic, Molecular, and Taxonomic Evolution of Renal Cell Carcinoma: A Conceptual Perspective With Emphasis on Updates to the 2016 World Health Organization Classification
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PTPMT1 Inhibition Lowers Glucose through Succinate Dehydrogenase Phosphorylation
Nath, A. K., Ryu, J. H., Jin, Y. N., Roberts, L. D., Dejam, A., Gerszten, R. E., & Peterson, R. T. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.010 · Cited by 62 · see citing works
Aberrant DNA hypermethylation of SDHC: a novel mechanism of tumor development in Carney triad
Haller, F., Moskalev, E. A., Faucz, F. R., Barthelmesz, S., Wiemann, S., Bieg, M., Assié, G., Bertherat, J. Y., Schaefer, I., Otto, C., et al. (2015) · Endocrine Abstracts · doi:10.1530/endoabs.38.ja3 · Cited by 62 · see citing works
Identification of the flavoprotein of succinate dehydrogenase and aconitase as in vitro mitochondrial substrates of Fgr tyrosine kinase
Salvi, M., MORRICE, N. A., Brunati, A. M., & Toninello, A. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.005 · Cited by 61 · see citing works
Gastrointestinal stromal tumor: Recent advances in pathology and genetics
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The Saccharomyces cerevisiae succinate dehydrogenase does not require heme for ubiquinone reduction
Oyedotun, K. S., Sit, C. S., & Lemire, B. D. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.09.008 · Cited by 54 · see citing works
Epigenetic Mutation of the Succinate Dehydrogenase C Promoter in a Patient With Two Paragangliomas
Richter, S., Klink, B., Nacke, B., de Cubas, A. A., Mangelis, A., Rapizzi, E., Meinhardt, M., Skondra, C. D., Mannelli, M., Robledo, M., et al. (2015) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-3856 · Cited by 53 · see citing works
Renal carcinoma associated with a novel succinate dehydrogenase A mutation: a case report and review of literature of a rare subtype of renal carcinoma
Özlük, Y., Taheri, D., Matoso, A., Şanlı, Ö., Berker, N. K., Yakirevich, E., Balasubramanian, S., Ross, J. S., Ali, S. M., & Netto, G. J. (2015) · Human Pathology · doi:10.1016/j.humpath.2015.07.027 · Cited by 51 · see citing works
Escherichia coli succinate dehydrogenase variant lacking the heme b
Tran, Q. M., Rothery, R. A., Maklashina, E., Cecchini, G., & Weiner, J. H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707732104 · Cited by 51 · see citing works
Gatekeepers of chromatin: Small metabolites elicit big changes in gene expression
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Familial pheochromocytomas and paragangliomas
King, K. S., & Pacák, K. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.07.032 · Cited by 49 · see citing works
Mitochondrial matrix proteostasis is linked to hereditary paraganglioma: LON‐mediated turnover of the human flavinylation factor SDH5 is regulated by its interaction with SDHA
Bezawork‐Geleta, A., Saiyed, T., Dougan, D. A., & Truscott, K. N. (2014) · The FASEB Journal · doi:10.1096/fj.13-242420 · Cited by 42 · see citing works
Self-citation
Succinate Dehydrogenase Gene Mutations in Cardiac Paragangliomas
Martucci, V. L., Emaminia, A., Rivero, J. D., Lechan, R. M., Magoon, B. T., Galia, A., Fojo, T., Leung, S., Lorusso, R., Jiménez, C., et al. (2015) · The American Journal of Cardiology · doi:10.1016/j.amjcard.2015.03.020 · Cited by 41 · see citing works
SDHC mutation in an elderly patient without familial antecedents
López-Jiménez, E. A., de Campos, J. M., Kusak, E., Landa, I., Leskelä, S., Montero‐Conde, C., Leandro-Garcia, L. J., Vallejo, L. A., Madrigal, B., Rodríguez‐Antona, C., et al. (2008) · Clinical Endocrinology · doi:10.1111/j.1365-2265.2008.03368.x · Cited by 41 · see citing works
Manganese ions induce H2O2 generation at the ubiquinone binding site of mitochondrial complex II
Bonke, E., Zwicker, K., & Dröse, S. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.06.011 · Cited by 39 · see citing works
Universal Genetic Screening Uncovers a Novel Presentation of an SDHAF2 Mutation
Casey, R. T., Garrahy, A., Tuthill, A., O’Halloran, D., Joyce, C. M., Casey, M. B., O’Shea, P. M., & Bell, M. (2014) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-4536 · Cited by 39 · see citing works
Renal Carcinoma Associated With Succinate Dehydrogenase B Mutation: A New and Unique Subtype of Renal Carcinoma
Paik, J. Y., Toon, C. W., Benn, D. E., High, H. A., Hasovitz, C., Pavlakis, N., Clifton-Bligh, R. J., & Gill, A. J. (2014) · Journal of Clinical Oncology · doi:10.1200/jco.2012.47.2647 · Cited by 34 · see citing works
SDHC methylation in gastrointestinal stromal tumors (GIST): a case report
Urbini, M., Astolfi, A., Indio, V., Heinrich, M. C., Corless, C. L., Nannini, M., Ravegnini, G., Biasco, G., & Pantaleo, M. A. (2015) · BMC Medical Genetics · doi:10.1186/s12881-015-0233-7 · Cited by 29 · see citing works
The Assembly Factor SDHAF2 Is Dispensable for Flavination of the Catalytic Subunit of Mitochondrial Complex II in Breast Cancer Cells
Bezawork‐Geleta, A., Dong, L., Rohlena, J., & Neužil, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.c116.755017 · Cited by 26 · see citing works
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Epigenetic methylations and their connections with metabolism
Chiacchiera, F., Piunti, A., & Pasini, D. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1293-5 · Cited by 24 · see citing works
Vitamin E Protects against Lipid Peroxidation and Rescues Tumorigenic Phenotypes in Cowden/Cowden-like Patient-Derived Lymphoblast Cells with Germline SDHx Variants
Ni, Y., & Eng, C. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-1055 · Cited by 23 · see citing works
Analysis of covalent flavinylation using thermostable succinate dehydrogenase from Thermus thermophilus and Sulfolobus tokodaii lacking SdhE homologs
Kounosu, A. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.02.022 · Cited by 20 · see citing works

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Mitochondrial electron transport chain, ROS generation and uncoupling (Review)
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The Itaconate Pathway Is a Central Regulatory Node Linking Innate Immune Tolerance and Trained Immunity
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Targeting Metabolic–Redox Circuits for Cancer Therapy
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Mitochondrial complex II and reactive oxygen species in disease and therapy
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Early Events in Plant Abiotic Stress Signaling: Interplay Between Calcium, Reactive Oxygen Species and Phytohormones
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Structural basis of mitochondrial membrane bending by the I–II–III2–IV2 supercomplex
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Cadmium-Induced Cytotoxicity: Effects on Mitochondrial Electron Transport Chain
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Assembly of the Complexes of the Oxidative Phosphorylation System in Land Plant Mitochondria
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Lysosomal Signaling Promotes Longevity by Adjusting Mitochondrial Activity
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Regulation of Mitochondrial Electron Transport Chain Assembly
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Role of Metabolism in Bone Development and Homeostasis
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Reactive Oxygen Species: Not Omnipresent but Important in Many Locations
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SDHi fungicides: An example of mitotoxic pesticides targeting the succinate dehydrogenase complex
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Mitochondrial Reactive Oxygen Species in Infection and Immunity
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Superiority of 68Ga-DOTATATE over 18F-FDG and anatomic imaging in the detection of succinate dehydrogenase mutation (SDHx )-related pheochromocytoma and paraganglioma in the pediatric population
Jha, A., Ling, A. L., Millo, C., Gupta, G., Viana, B., Lin, F. I., Herscovitch, P., Adams, K. T., Taïeb, D., Metwalli, A. R., et al. (2017) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-017-3896-9 · Cited by 87 · see citing works
Mitochondrial complex II of plants: subunit composition, assembly, and function in respiration and signaling
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Free radicals: Relationship to Human Diseases and Potential Therapeutic applications
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Molecular and Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System: Implications for Pathology
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Breast cancer–associated macrophages promote tumorigenesis by suppressing succinate dehydrogenase in tumor cells
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Impairment of mitochondrial function by particulate matter: Implications for the brain
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Alternative assembly of respiratory complex II connects energy stress to metabolic checkpoints
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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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