The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target is correctly identified: Sdhaf2 in Mus musculus encodes succinate dehydrogenase complex assembly factor 2, matching the supplied UniProt accession A0A494B8X4, Ensembl protein ENSMUSP00000157391.2, and MGI identifier MGI:1913322. The supplied InterPro/Pfam annotations—SDH-related fold IPR005631/IPR036714 and Sdh5 family PF03937—are consistent with the conserved eukaryotic SDHAF2/Sdh5 and bacterial SdhE assembly-factor family. No conflicting mouse gene with the same symbol was identified.
The best-supported primary annotation is: a nuclear-encoded mitochondrial SDHA maturation and complex-II assembly factor. Sdhaf2 is not a succinate-metabolizing enzyme itself and has no established independently catalyzed reaction. It transiently binds the flavoprotein subunit SDHA, promotes acquisition and covalent incorporation of FAD, and thereby supports assembly of catalytically competent succinate dehydrogenase/respiratory complex II. Direct mouse evidence is strongest in skeletal muscle and murine myocytes; detailed chemistry derives mainly from human, yeast, and bacterial orthologs.
| Annotation claim | Conclusion | Strongest evidence system | Confidence | Key caveat |
|---|---|---|---|---|
| Identity | Sdhaf2 is the mouse gene encoding succinate dehydrogenase complex assembly factor 2, consistent with UniProt A0A494B8X4 and the conserved Sdh5/PF03937 family. | Direct mouse annotation and cross-species conservation | High | Most detailed biochemical studies concern human or microbial orthologs rather than this exact mouse proteoform. |
| Mitochondrial localization | Mouse Sdhaf2 acts in mitochondria. Drp1 deficiency lowers Sdhaf2 in mouse-muscle mitochondrial fractions without eliminating total Sdhaf2, consistent with regulated mitochondrial translocation (zhou2024drp1controlscomplex pages 5-8, zhou2024drp1controlscomplex pages 8-10). | Direct mouse in vivo and murine C2C12 cells | High | Fractionation and colocalization establish mitochondrial association but do not directly resolve matrix versus inner-membrane-facing topology. |
| SDHA binding | SDHAF2 physically associates with SDHA during maturation; purified recombinant human SDHA remains tightly associated with SDHAF2 (maklashina2018theunassembledflavoprotein pages 18-20, maklashina2018theunassembledflavoprotein pages 1-2). | Human biochemistry | High for conserved mammalian function | Direct biochemical binding has not been demonstrated for UniProt A0A494B8X4 itself. |
| Promotion of covalent FAD flavinylation | SDHAF2 promotes maturation of SDHA containing covalently bound FAD. Human SDHA expressed in bacteria was fully flavinylated only with human SDHAF2, while conserved microbial SdhE/Sdh5 mutations disrupt flavinylation (maklashina2018theunassembledflavoprotein pages 1-2, hensen2011recentadvancesin pages 2-4, mcneil2013theconservedrgxxe pages 10-11). | Human biochemistry and yeast/bacterial conservation | High for a facilitating role | SDHAF2 is not proven to catalyze covalent-bond formation directly; SDHA flavinylation can occur without it in some mammalian contexts (chen2024sdhaf2facilitatesmitochondrial pages 1-3). |
| Complex II assembly and activity | Sdhaf2 supports complex II assembly and function. Reduced mitochondrial Sdhaf2 in Drp1-deficient mouse muscle accompanies selective assembly defects, reduced succinate-supported respiration, and succinate accumulation; Sdhaf2 restoration rescues complex-II-linked functions in murine myocytes (zhou2024drp1controlscomplex pages 5-8, zhou2024drp1controlscomplex pages 8-10, zhou2024drp1controlscomplex pages 1-1, zhou2024drp1controlscomplex pages 3-5). | Direct mouse in vivo and murine C2C12 cells | High | The in vivo perturbation targeted Drp1 rather than Sdhaf2; rescue was performed principally in cultured myocytes. |
| Direct catalyzed reaction by SDHAF2 | No independent catalytic reaction or substrate turnover is established. Sdhaf2 is a transient SDHA assembly/maturation factor, not a metabolic enzyme or stable catalytic subunit of mature complex II (maklashina2018theunassembledflavoprotein pages 1-2, estebanamo2026pleiotropicimpactof pages 1-4). | Human biochemistry and conserved assembly biology | High | The molecular mechanism by which SDHAF2 assists FAD incorporation and covalent attachment remains incompletely resolved. |
| Downstream complex II reaction | By enabling complex II maturation, Sdhaf2 indirectly supports succinate + ubiquinone → fumarate + ubiquinol. SDHA oxidizes succinate through FAD, electrons traverse SDHB iron–sulfur centers, and SDHC/SDHD reduce ubiquinone; complex II does not pump protons (iverson2023anevolvingview pages 1-2, estebanamo2024succinatedehydrogenaseand pages 1-2). | Structural and biochemical consensus | High | Complex II, not Sdhaf2, catalyzes this reaction; reverse fumarate reduction can occur under highly reduced or oxygen-limited conditions (iverson2023anevolvingview pages 10-11). |
| Mouse knockout and organismal phenotype | No well-characterized dedicated whole-body or conditional Sdhaf2 knockout phenotype was identified. Mouse evidence mainly links altered Sdhaf2 mitochondrial trafficking to muscle complex II defects, lipid accumulation, reduced fatty-acid oxidation, and impaired insulin action (zhou2024drp1controlscomplex pages 5-8, zhou2024drp1controlscomplex pages 1-1, zhou2024drp1controlscomplex pages 1-3). | Direct mouse in vivo, with indirect Sdhaf2 perturbation | Moderate | Phenotypes from Drp1 deficiency or other SDHx models cannot be attributed uniquely to Sdhaf2; dedicated allele-specific mouse studies are needed. |
Table: Evidence-weighted functional annotations for mouse Sdhaf2 distinguish direct mouse findings from mechanistic inference based on murine cells, human biochemistry, and conserved microbial systems.
The symbol and description are concordant: mouse Sdhaf2 is orthologous to human SDHAF2, yeast Sdh5, and bacterial SdhE. Literature sometimes uses “SDH5,” particularly for the yeast protein or historically for the human disease gene; this is not a different functional target. Conserved bacterial mutagenesis maps the disease-relevant human Gly78 region onto the RGxxE functional motif of SdhE, supporting genuine family-level homology rather than a merely similar name (mcneil2013theconservedrgxxe pages 10-11).
The database record supplied by the user appears to be an Ensembl-derived UniProt entry and may not be the best curated canonical mouse proteoform. Consequently, sequence-length, isoform, or residue-level statements should remain tied to A0A494B8X4 rather than transferred automatically from human SDHAF2. Nevertheless, gene identity, organism, domain family, and primary functional annotation all align; there is no reason to stop because of symbol ambiguity.
Sdhaf2 is best described as an SDHA-specific maturation/assembly factor. It associates transiently with SDHA before SDHA joins SDHB and the membrane-anchor subunits SDHC/SDHD. A recognized low-molecular-mass assembly intermediate contains flavinated SDHA associated with SDHAF2; the factor is not considered a permanent stoichiometric subunit of mature complex II (estebanamo2026pleiotropicimpactof pages 1-4).
Purified recombinant human SDHA remains tightly associated with human SDHAF2, and mass spectrometry confirms SDHAF2 in this preparation. Human SDHA expressed in bacteria became fully flavinylated only when coexpressed with human SDHAF2; endogenous bacterial SdhE could not substitute effectively. This provides strong biochemical evidence for a specific SDHA–SDHAF2 interaction and a conserved mammalian maturation role, although it is not an experiment on A0A494B8X4 itself (maklashina2018theunassembledflavoprotein pages 18-20, maklashina2018theunassembledflavoprotein pages 1-2).
SDHA contains the succinate-binding catalytic site and a covalently attached FAD prosthetic group. SDHAF2 facilitates FAD acquisition and covalent flavinylation of SDHA, which promotes formation of active complex II. The human p.Gly78Arg disease variant has been associated with loss of SDHA flavinylation and complex-II activity, while analogous bacterial substitutions disrupt SdhA flavinylation, supporting evolutionary conservation of this function (hensen2011recentadvancesin pages 2-4, mcneil2013theconservedrgxxe pages 10-11).
An important qualification is that SDHAF2 has not been definitively shown to be an FAD-transferase or covalent-bond-forming enzyme. The biochemical mechanism may involve stabilizing an SDHA conformation favorable for FAD binding, positioning FAD and/or succinate, or protecting a maturation intermediate. Bacterial motif experiments show that some substitutions preserve SDHA interaction yet disrupt flavinylation or activation, indicating that binding alone is insufficient. Moreover, mammalian work has reported some SDHA flavinylation in the absence of SDHAF2. The current interpretation is therefore that SDHAF2 strongly facilitates efficient flavinylation and assembly, not that it is invariably the direct catalyst of the covalent attachment reaction (chen2024sdhaf2facilitatesmitochondrial pages 1-3, mcneil2013theconservedrgxxe pages 10-11).
There is no independently established substrate-turnover reaction for Sdhaf2. Its functional client is SDHA, and FAD is the cofactor whose productive incorporation it promotes.
The downstream reaction catalyzed by the assembled complex is:
succinate + ubiquinone → fumarate + ubiquinol.
SDHA oxidizes succinate to fumarate through FAD; electrons then pass through SDHB’s three iron–sulfur clusters to the SDHC/SDHD membrane module, where ubiquinone is reduced. Complex II thus links the tricarboxylic-acid cycle to the electron-transport chain. Unlike complexes I, III, and IV, it does not pump protons across the inner mitochondrial membrane (iverson2023anevolvingview pages 1-2, estebanamo2024succinatedehydrogenaseand pages 1-2).
Under oxygen-limited conditions or when the ubiquinone pool is highly reduced, complex II can operate in reverse, using fumarate as an electron acceptor and producing succinate. This reverse activity is context- and tissue-dependent and should be attributed to complex II, not to Sdhaf2 directly (iverson2023anevolvingview pages 10-11).
The gene is nuclear encoded, whereas its protein product functions inside mitochondria. Because its client SDHA is the matrix-exposed catalytic subunit of inner-membrane complex II, the most plausible operative compartment is the mitochondrial matrix or matrix face of the inner membrane during assembly. The literature retrieved here strongly establishes mitochondrial localization but does not provide a definitive submitochondrial-topology experiment for A0A494B8X4.
Direct mouse evidence comes from skeletal-muscle fractionation. Drp1-deficient mouse muscle retained total Sdhaf2 but had selectively reduced Sdhaf2 in mitochondrial fractions, while murine C2C12 cells showed Drp1–Sdhaf2 colocalization and Drp1-dependent mitochondrial targeting. These observations support regulated mitochondrial delivery or retention rather than simple transcriptional loss (zhou2024drp1controlscomplex pages 5-8, zhou2024drp1controlscomplex pages 8-10).
Sdhaf2 participates in:
Unassembled human SDHA–SDHAF2 has approximately 25-fold lower activity in the reported isolated preparation, and unassembled SDHA produces only minor ROS. Robust catalysis therefore requires later assembly with the SDHB iron–sulfur subunit and membrane module; SDHAF2-assisted flavinylation is necessary but not by itself sufficient for full succinate:ubiquinone oxidoreductase activity (maklashina2018theunassembledflavoprotein pages 18-20, maklashina2018theunassembledflavoprotein pages 1-2).
The most informative mouse-focused study is Zhou et al., published 3 April 2024 in Science Advances, DOI/URL: https://doi.org/10.1126/sciadv.adl0389. Muscle-specific Drp1 deficiency caused a selective complex-II defect: succinate-plus-rotenone-supported respiration was reduced, whereas pyruvate-plus-malate respiration was preserved. Blue-native PAGE showed impaired complex-II assembly without equivalent reductions in complexes I, III, or IV (zhou2024drp1controlscomplex pages 5-8, zhou2024drp1controlscomplex pages 3-5).
In muscle-specific Drp1-heterozygous mice, Drp1 protein was reduced by approximately 30%. These mice had mitochondrial elongation, elevated muscle succinate, impaired glucose homeostasis and insulin action, reduced ex-vivo insulin-stimulated soleus glucose uptake, higher respiratory-exchange ratio, lower oxygen consumption and energy expenditure, elevated plasma lactate, and accumulation of several intramuscular lipid classes (zhou2024drp1controlscomplex pages 1-3).
Mechanistically, SDHA and SDHB abundance remained largely unchanged, but mitochondrial Sdhaf2 was reduced. BN-PAGE comparisons used five mice per genotype. In obese Ob/+ mice, Drp1 was reduced by approximately 60%; total-muscle Sdhaf2 increased while mitochondrial Sdhaf2 decreased, accompanied by abnormal complex-II architecture. These data argue that localization, rather than total abundance alone, controls Sdhaf2 function (zhou2024drp1controlscomplex pages 5-8).
In murine C2C12 myocytes, restoring Sdhaf2 in Drp1-knockdown cells rescued succinate-linked respiratory control, fatty-acid oxidation, insulin-stimulated Akt Ser473 phosphorylation, and extracellular-lactate abnormalities. Typical replicate numbers were n=3 for immunoblots and insulin/Akt assays, n=4 for fatty-acid oxidation, and n=4–5 for respiratory measurements; significance was assessed by two-tailed tests with P<0.05 (zhou2024drp1controlscomplex pages 8-10).
These are compelling functional data, but attribution must be precise: the in-vivo initiating perturbation was Drp1 deficiency, not an Sdhaf2 knockout, and the Sdhaf2 rescue was primarily performed in cultured murine myocytes. Thus, this study establishes that mouse Sdhaf2 availability within mitochondria is sufficient to explain an important component of the complex-II and metabolic phenotype, but not the full organismal phenotype of isolated Sdhaf2 loss.
No well-characterized whole-body or tissue-specific Sdhaf2-null mouse study was identified in the retrieved literature. Therefore, embryonic viability, fertility, neurological effects, tumor penetrance, and lifespan cannot be assigned confidently to mouse Sdhaf2. Phenotypes from Sdhd, Sdhc, Sdhaf4, or Drp1 models are mechanistically informative but are not substitutes for an Sdhaf2 allele-specific model.
Chen et al., published November 2024 in Mitochondrion, DOI/URL: https://doi.org/10.1016/j.mito.2024.101952, used human HeLa cells. SDHAF2 knockout impaired basal and maximal respiration, complex-II activity, and complex-II assembly despite preserved SDHA and SDHB abundance; complementation rescued these abnormalities. Approximately 20% of knockout cells lost mitochondrial membrane-potential signals, indicating that generalized depolarization did not explain most respiratory defects (chen2024sdhaf2facilitatesmitochondrial pages 6-8).
Unexpectedly, SDHAF2 loss also reduced complex-IV activity and assembly. Acute or chronic pharmacological SDH inhibition and SDHD knockout did not reproduce this complex-IV phenotype, leading the authors to propose an SDH-independent role for SDHAF2 in cytochrome-c-oxidase assembly or stability. This is a significant recent development, but it remains human-cell evidence and should not yet be considered an established function of mouse A0A494B8X4 (chen2024sdhaf2facilitatesmitochondrial pages 6-8).
Iverson, Singh, and Cecchini’s review, published online 27 April 2023 and in the June 2023 issue of Journal of Biological Chemistry, DOI/URL: https://doi.org/10.1016/j.jbc.2023.104761, emphasizes that complex II participates not only in canonical succinate oxidation but also in reverse electron flow, noncanonical assemblies, ROS and metabolite signaling, inflammation, and cell-fate regulation (iverson2023anevolvingview pages 1-2, iverson2023anevolvingview pages 10-11).
Esteban-Amo et al., published 9 September 2024 in Biomedicines, DOI/URL: https://doi.org/10.3390/biomedicines12092050, similarly places complex II at the TCA–OXPHOS interface and estimates congenital SDH deficiencies at approximately 2% of mitochondrial-disease diagnoses. This statistic concerns all SDH deficiencies, not Sdhaf2 specifically (estebanamo2024succinatedehydrogenaseand pages 1-2).
Human SDHAF2 pathogenic variants cause a rare hereditary paraganglioma predisposition, classically involving head-and-neck paragangliomas and a parent-of-origin effect. The recurrent p.Gly78Arg allele links defective SDHA flavinylation to loss of SDH activity. In one follow-up cohort of 443 patients, no SDHAF2 mutations were identified among pheochromocytoma cases, illustrating that SDHAF2 is a rare contributor even within SDH-associated tumor syndromes (hensen2011recentadvancesin pages 2-4).
The practical applications are currently indirect:
There is no established approved therapy that directly activates or replaces SDHAF2. Manipulating Sdhaf2 localization or stabilizing the SDHA–SDHAF2 intermediate is a plausible research strategy, but remains preclinical.
High-confidence annotation: mouse Sdhaf2 is a mitochondrial SDHA maturation factor required for efficient complex-II assembly and activity. Its strongest mechanistic role is promotion of FAD incorporation/covalent SDHA flavinylation through direct or transient interaction with SDHA.
High-confidence negative annotation: Sdhaf2 is not itself succinate dehydrogenase, does not directly oxidize succinate, and is not a stable catalytic subunit of mature complex II.
Moderate-confidence refinement: the operative submitochondrial location is the matrix/matrix-facing assembly environment, but direct topology data for A0A494B8X4 are limited.
Emerging function: stabilization of complex IV may represent a second mammalian function, but this is presently based on 2024 human-cell evidence and requires independent confirmation in mouse tissues (chen2024sdhaf2facilitatesmitochondrial pages 6-8).
Principal evidence gap: a dedicated Sdhaf2 mouse knockout or endogenous separation-of-function allele with measurements of SDHA flavinylation, complex-II assembly, tissue metabolism, and organismal phenotype. Until such data are available, human and microbial biochemical mechanisms should be labeled as strong orthology-based inference rather than direct proof for every feature of UniProt A0A494B8X4.
References
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(zhou2024drp1controlscomplex pages 8-10): Zhenqi Zhou, Alice Ma, Timothy M. Moore, Dane M. Wolf, Nicole Yang, Peter Tran, Mayuko Segawa, Alexander R. Strumwasser, Wenjuan Ren, Kai Fu, Jonathan Wanagat, Alexander M. van der Bliek, Rachelle Crosbie-Watson, Marc Liesa, Linsey Stiles, Rebecca Acin-Perez, Sushil Mahata, Orian Shirihai, Mark O. Goodarzi, Michal Handzlik, Christian M. Metallo, David W. Walker, and Andrea L. Hevener. Drp1 controls complex ii assembly and skeletal muscle metabolism by sdhaf2 action on mitochondria. Apr 2024. URL: https://doi.org/10.1126/sciadv.adl0389, doi:10.1126/sciadv.adl0389. This article has 30 citations and is from a highest quality peer-reviewed journal.
(maklashina2018theunassembledflavoprotein pages 18-20): Elena Maklashina, Sany Rajagukguk, T.M. Iverson, and Gary Cecchini. The unassembled flavoprotein subunits of human and bacterial complex ii have impaired catalytic activity and generate only minor amounts of ros. May 2018. URL: https://doi.org/10.1074/jbc.ra118.001977, doi:10.1074/jbc.ra118.001977. This article has 38 citations and is from a domain leading peer-reviewed journal.
(maklashina2018theunassembledflavoprotein pages 1-2): Elena Maklashina, Sany Rajagukguk, T.M. Iverson, and Gary Cecchini. The unassembled flavoprotein subunits of human and bacterial complex ii have impaired catalytic activity and generate only minor amounts of ros. May 2018. URL: https://doi.org/10.1074/jbc.ra118.001977, doi:10.1074/jbc.ra118.001977. This article has 38 citations and is from a domain leading peer-reviewed journal.
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(mcneil2013theconservedrgxxe pages 10-11): Matthew B. McNeil and Peter C. Fineran. The conserved rgxxe motif of the bacterial fad assembly factor sdhe is required for succinate dehydrogenase flavinylation and activity. Biochemistry, 52 43:7628-40, Oct 2013. URL: https://doi.org/10.1021/bi401006a, doi:10.1021/bi401006a. This article has 27 citations and is from a peer-reviewed journal.
(chen2024sdhaf2facilitatesmitochondrial pages 1-3): Chang-Lin Chen, Takaya Ishihara, Soumyadip Pal, Wei-Ling Huang, Emi Ogasawara, Chuang-Rung Chang, and Naotada Ishihara. Sdhaf2 facilitates mitochondrial respiration through stabilizing succinate dehydrogenase and cytochrome c oxidase assemblies. Nov 2024. URL: https://doi.org/10.1016/j.mito.2024.101952, doi:10.1016/j.mito.2024.101952. This article has 21 citations and is from a peer-reviewed journal.
(zhou2024drp1controlscomplex pages 1-1): Zhenqi Zhou, Alice Ma, Timothy M. Moore, Dane M. Wolf, Nicole Yang, Peter Tran, Mayuko Segawa, Alexander R. Strumwasser, Wenjuan Ren, Kai Fu, Jonathan Wanagat, Alexander M. van der Bliek, Rachelle Crosbie-Watson, Marc Liesa, Linsey Stiles, Rebecca Acin-Perez, Sushil Mahata, Orian Shirihai, Mark O. Goodarzi, Michal Handzlik, Christian M. Metallo, David W. Walker, and Andrea L. Hevener. Drp1 controls complex ii assembly and skeletal muscle metabolism by sdhaf2 action on mitochondria. Apr 2024. URL: https://doi.org/10.1126/sciadv.adl0389, doi:10.1126/sciadv.adl0389. This article has 30 citations and is from a highest quality peer-reviewed journal.
(zhou2024drp1controlscomplex pages 3-5): Zhenqi Zhou, Alice Ma, Timothy M. Moore, Dane M. Wolf, Nicole Yang, Peter Tran, Mayuko Segawa, Alexander R. Strumwasser, Wenjuan Ren, Kai Fu, Jonathan Wanagat, Alexander M. van der Bliek, Rachelle Crosbie-Watson, Marc Liesa, Linsey Stiles, Rebecca Acin-Perez, Sushil Mahata, Orian Shirihai, Mark O. Goodarzi, Michal Handzlik, Christian M. Metallo, David W. Walker, and Andrea L. Hevener. Drp1 controls complex ii assembly and skeletal muscle metabolism by sdhaf2 action on mitochondria. Apr 2024. URL: https://doi.org/10.1126/sciadv.adl0389, doi:10.1126/sciadv.adl0389. This article has 30 citations and is from a highest quality peer-reviewed journal.
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(iverson2023anevolvingview pages 1-2): T.M. Iverson, Prashant K. Singh, and Gary Cecchini. An evolving view of complex ii—noncanonical complexes, megacomplexes, respiration, signaling, and beyond. Jun 2023. URL: https://doi.org/10.1016/j.jbc.2023.104761, doi:10.1016/j.jbc.2023.104761. This article has 63 citations and is from a domain leading peer-reviewed journal.
(estebanamo2024succinatedehydrogenaseand pages 1-2): María J. Esteban-Amo, Patricia Jiménez-Cuadrado, Pablo Serrano-Lorenzo, Miguel Á. de la Fuente, and María Simarro. Succinate dehydrogenase and human disease: novel insights into a well-known enzyme. Sep 2024. URL: https://doi.org/10.3390/biomedicines12092050, doi:10.3390/biomedicines12092050. This article has 48 citations.
(iverson2023anevolvingview pages 10-11): T.M. Iverson, Prashant K. Singh, and Gary Cecchini. An evolving view of complex ii—noncanonical complexes, megacomplexes, respiration, signaling, and beyond. Jun 2023. URL: https://doi.org/10.1016/j.jbc.2023.104761, doi:10.1016/j.jbc.2023.104761. This article has 63 citations and is from a domain leading peer-reviewed journal.
(zhou2024drp1controlscomplex pages 1-3): Zhenqi Zhou, Alice Ma, Timothy M. Moore, Dane M. Wolf, Nicole Yang, Peter Tran, Mayuko Segawa, Alexander R. Strumwasser, Wenjuan Ren, Kai Fu, Jonathan Wanagat, Alexander M. van der Bliek, Rachelle Crosbie-Watson, Marc Liesa, Linsey Stiles, Rebecca Acin-Perez, Sushil Mahata, Orian Shirihai, Mark O. Goodarzi, Michal Handzlik, Christian M. Metallo, David W. Walker, and Andrea L. Hevener. Drp1 controls complex ii assembly and skeletal muscle metabolism by sdhaf2 action on mitochondria. Apr 2024. URL: https://doi.org/10.1126/sciadv.adl0389, doi:10.1126/sciadv.adl0389. This article has 30 citations and is from a highest quality peer-reviewed journal.
(chen2024sdhaf2facilitatesmitochondrial pages 6-8): Chang-Lin Chen, Takaya Ishihara, Soumyadip Pal, Wei-Ling Huang, Emi Ogasawara, Chuang-Rung Chang, and Naotada Ishihara. Sdhaf2 facilitates mitochondrial respiration through stabilizing succinate dehydrogenase and cytochrome c oxidase assemblies. Nov 2024. URL: https://doi.org/10.1016/j.mito.2024.101952, doi:10.1016/j.mito.2024.101952. This article has 21 citations and is from a peer-reviewed journal.