SDHAF1

Last update 08 May 2025

Basic Info

Synonyms

LYR motif-containing protein 8, LYRM8, SDH assembly factor 1

+ [3]

Introduction

Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol (PubMed:19465911, PubMed:24954417). Promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants (PubMed:24954417). May act together with SDHAF3 (PubMed:24954417). Contributes to iron-sulfur cluster incorporation into SDHB by binding to SDHB and recruiting the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20 (PubMed:26749241).

100 Clinical Results associated with SDHAF1

100 Translational Medicine associated with SDHAF1

0 Patents (Medical) associated with SDHAF1

Literatures (Medical) associated with SDHAF1

01 Dec 2024·Molecular Biology Reports

Differential expression of nuclear-derived mitochondrial succinate dehydrogenase genes in metabolically active buffalo tissues

Article

Author: Sadeesh, E M ; Sadeesh, E. M. ; Singh, Pratiksha ; Lahamge, Madhuri S. ; Lahamge, Madhuri S ; Malik, Anuj

BACKGROUNDBuffaloes are crucial to agriculture, yet mitochondrial biology in these animals is less studied compared to humans and laboratory animals. This research examines tissue-specific variations in mitochondrial succinate dehydrogenase (SDH) gene expression across buffalo kidneys, hearts, brains, and ovaries. Understanding these variations sheds light on mitochondrial energy metabolism and its impact on buffalo health and productivity, revealing insights into enzyme regulation and potential improvements in livestock management.MATERIALS AND METHODSRNA-seq data from buffalo kidney, heart, brain, and ovary tissues were reanalyzed to explore mitochondrial SDH gene expression. The expression of SDH subunits (SDHA, SDHB, SDHC, SDHD) and assembly factors (SDHAF1, SDHAF2, SDHAF3, SDHAF4) was assessed using a log2 fold-change threshold of + 1 for up-regulated and - 1 for down-regulated transcripts, with significance set at p < 0.05. Hierarchical clustering and differential expression analyses were performed to identify tissue-specific expression patterns and regulatory mechanisms, while Gene Ontology and KEGG pathway analyses were conducted to uncover functional attributes and pathway enrichments across different tissues.RESULTSReanalysis of RNA-seq data from different tissues of healthy female buffaloes revealed distinct expression patterns for SDH subunits and assembly factors. While SDHA, SDHB, and SDHC showed variable expression across tissues, SDHAF2, SDHAF3, and SDHAF4 exhibited tissue-specific profiles. Significant up-regulation of SDHA, SDHB, and several assembly factors was observed in specific tissue comparisons, with fewer down-regulated transcripts. Gene ontology and KEGG pathway analyses linked the up-regulated transcripts to mitochondrial ATP synthesis and the respiratory electron transport chain. Notably, tissue-specific variations in mitochondrial function were particularly evident in the ovary.CONCLUSIONThis study identifies distinct SDH gene expression patterns in buffalo tissues, highlighting significant down-regulation of SDHA, SDHB, SDHC, and assembly factors in the ovary. These findings underscore the critical role of mitochondria in tissue-specific energy production and metabolic regulation, suggest potential metabolic adaptations, and emphasize the importance of mitochondrial complex II. The insights gained offer valuable implications for improving feed efficiency and guiding future research and therapies for energy metabolism disorders.

01 Aug 2024·Cell Stem Cell

SDHAF1 confers metabolic resilience to aging hematopoietic stem cells by promoting mitochondrial ATP production

Article

Author: Sumiyama, Kenta ; Nakamura-Ishizu, Ayako ; Suda, Toshio ; Fujita, Shinya ; Nakano, Hiroyasu ; Kondoh, Hiroshi ; Karigane, Daiki ; Shide, Kotaro ; Nagamatsu, Go ; Shiroshita, Kohei ; Okamoto, Shinichiro ; Sugiura, Yuki ; Shimoda, Kazuya ; Takubo, Keiyo ; Watanuki, Shintaro ; Yamamoto, Masamichi ; Haraguchi, Miho ; Morikawa, Takayuki ; Sorimachi, Yuriko ; Mikawa, Takumi ; Goda, Nobuhito ; Suematsu, Makoto ; Tamaki, Shinpei ; Kobayashi, Hiroshi

Aging generally predisposes stem cells to functional decline, impairing tissue homeostasis. Here, we report that hematopoietic stem cells (HSCs) acquire metabolic resilience that promotes cell survival. High-resolution real-time ATP analysis with glucose tracing and metabolic flux analysis revealed that old HSCs reprogram their metabolism to activate the pentose phosphate pathway (PPP), becoming more resistant to oxidative stress and less dependent on glycolytic ATP production at steady state. As a result, old HSCs can survive without glycolysis, adapting to the physiological cytokine environment in bone marrow. Mechanistically, old HSCs enhance mitochondrial complex II metabolism during stress to promote ATP production. Furthermore, increased succinate dehydrogenase assembly factor 1 (SDHAF1) in old HSCs, induced by physiological low-concentration thrombopoietin (TPO) exposure, enables rapid mitochondrial ATP production upon metabolic stress, thereby improving survival. This study provides insight into the acquisition of resilience through metabolic reprogramming in old HSCs and its molecular basis to ameliorate age-related hematopoietic abnormalities.

01 Apr 2024·Alzheimer's & Dementia

Genetic associations with dementia‐related proteinopathy: Application of item response theory

Article

Author: Gauthreaux, Kathryn ; Katsumata, Yuriko ; Nelson, Peter T. ; Shade, Lincoln M. P. ; Karanth, Shama D. ; Hohman, Timothy J. ; Mock, Charles ; Abner, Erin L. ; Farfel, Jose M. ; Kukull, Walter A. ; Schneider, Julie A. ; Wu, Xian ; Bennett, David A. ; Fardo, David W.

AbstractINTRODUCTIONAlthough dementia‐related proteinopathy has a strong negative impact on public health, and is highly heritable, understanding of the related genetic architecture is incomplete.METHODSWe applied multidimensional generalized partial credit modeling (GPCM) to test genetic associations with dementia‐related proteinopathies. Data were analyzed to identify candidate single nucleotide variants for the following proteinopathies: Aβ, tau, α‐synuclein, and TDP‐43.RESULTSFinal included data comprised 966 participants with neuropathologic and WGS data. Three continuous latent outcomes were constructed, corresponding to TDP‐43‐, Aβ/Tau‐, and α‐synuclein‐related neuropathology endophenotype scores. This approach helped validate known genotype/phenotype associations: for example, TMEM106B and GRN were risk alleles for TDP‐43 pathology; and GBA for α‐synuclein/Lewy bodies. Novel suggestive proteinopathy‐linked alleles were also discovered, including several (SDHAF1, TMEM68, and ARHGEF28) with colocalization analyses and/or high degrees of biologic credibility.DISCUSSIONA novel methodology using GPCM enabled insights into gene candidates for driving misfolded proteinopathies.Highlights

Latent factor scores for proteinopathies were estimated using a generalized partial credit model.

The three latent continuous scores corresponded well with proteinopathy severity.

Novel genes associated with proteinopathies were identified.

Several genes had high degrees of biologic credibility for dementia risk factors.

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SDHAF1

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