Dual regulation of SLC25A39 by AFG3L2 and iron controls mitochondrial glutathione homeostasis
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Abstract
Organelle transporters define metabolic compartmentalization, and how this metabolite transport process can be modulated is poorly explored. Here, we discovered that human SLC25A39, a mitochondrial transporter critical for mitochondrial glutathione uptake, is a short-lived protein under dual regulation at the protein level. Co-immunoprecipitation mass spectrometry and CRISPR knockout (KO) in mammalian cells identified that mitochondrial m-AAA protease AFG3L2 is responsible for degrading SLC25A39 through the matrix loop 1. SLC25A39 senses mitochondrial iron-sulfur cluster using four matrix cysteine residues and inhibits its degradation. SLC25A39 protein regulation is robust in developing and mature neurons. This dual transporter regulation, by protein quality control and metabolic sensing, allows modulating mitochondrial glutathione level in response to iron homeostasis, opening avenues for exploring regulation of metabolic compartmentalization. Neuronal SLC25A39 regulation connects mitochondrial protein quality control, glutathione, and iron homeostasis, which were previously unrelated biochemical features in neurodegeneration.
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Cites
Fiji: an open-source platform for biological-image analysis
Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2019 · Cited by 66,890 · see citing works
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Varadi, M., Anyango, S., Deshpande, M., Nair, S., Natassia, C., Yordanova, G., Yuan, D., Stroe, O., Wood, G., Laydon, A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1061 · Cited by 7,850 · see citing works
Meister, A., & Anderson, M. E. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.003431 · Cited by 5,694 · see citing works
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388 · see citing works
ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642 · see citing works
Rapid single-step induction of functional neurons from human pluripotent stem cells
Zhang, Y., Pak, C., Han, Y., Ahlenius, H., Zhang, Z., Chanda, S., Marro, S., Patzke, C., Acuna, C., Covy, J., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.05.029 · Cited by 1,644 · see citing works
Function and biogenesis of iron-sulphur proteins
Lill, R. (2009) · Nature · doi:10.1038/nature08301 · Cited by 1,167 · see citing works
The mitochondrial transporter family SLC25: Identification, properties and physiopathology
Palmieri, F. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.05.005 · Cited by 618 · see citing works
OpenCell: Endogenous tagging for the cartography of human cellular organization
Cho, N. H., Cheveralls, K. C., Brunner, A.-D., Kim, K., Michaelis, A. C., Raghavan, P., Kobayashi, H., Savy, L., Li, J. Y., Canaj, H., et al. (2022) · Science · doi:10.1126/science.abi6983 · Cited by 567 · see citing works
New roles for mitochondrial proteases in health, ageing and disease
Quirós, P. M., Langer, T., & López-Otı́n, C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3984 · Cited by 546 · see citing works
Absolute quantification of matrix metabolites reveals the dynamics of mitochondrial metabolism
Chen, W. W., Freinkman, E., Wang, T., Birsoy, K., & Sabatini, D. M. (2016) · Cell · doi:10.1016/j.cell.2016.07.040 · Cited by 500 · see citing works
Transcription factor-mediated differentiation of human iPSCs into neurons
Fernandopulle, M. S., Prestil, R., Grunseich, C., Wang, C., Gan, L., & Ward, M. E. (2018) · Current Protocols in Cell Biology · doi:10.1002/cpcb.51 · Cited by 461 · see citing works
Two Families of Chaperonin: Physiology and Mechanism
Horwich, A. L., Fenton, W. A., Chapman, E., & Farr, G. W. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.23.090506.123555 · Cited by 422 · see citing works
Wang, C., Ward, M. E., Chen, R., Liu, K., Tracy, T. E., Chen, X., Xie, M., Sohn, P. D., Ludwig, C., Meyer-Franke, A., et al. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.08.019 · Cited by 400 · see citing works
Signal Transduction by Mitochondrial Oxidants
Finkel, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.271999 · Cited by 390 · see citing works
Iron–sulfur cluster biogenesis and human disease
Rouault, T. A., & Tong, W. H. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.05.008 · Cited by 387 · see citing works
Systematic analysis of protein turnover in primary cells
Mathieson, T., Franken, H., Kosiński, J., Kurzawa, N., Zinn, N., Sweetman, G. M. A., Poeckel, D., Ratnu, V. S., Schramm, M., Becher, I., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03106-1 · Cited by 375 · see citing works
Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28
Bella, D. D., Lazzaro, F., Brusco, A., Plumari, M., Battaglia, G. S., Pastore, A., Finardi, A., Cagnoli, C., Tempia, F., Frontali, M., et al. (2010) · Nature Genetics · doi:10.1038/ng.544 · Cited by 345 · see citing works
Murphy, M. P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4289 · Cited by 341 · see citing works
Chemical Synthesis of Proteins
Nilsson, B. L., Soellner, M. B., & Raines, R. T. (2005) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.34.040204.144700 · Cited by 335 · see citing works
Arlt, H., Tauer, R., Feldmann, H., Neupert, W., & Langer, T. (1996) · Cell · doi:10.1016/s0092-8674(00)81271-4 · Cited by 323 · see citing works
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context
Morgenstern, M., Peikert, C. D., Lübbert, P., Suppanz, I., Klemm, C., Alka, O., Steiert, C., Naumenko, N., Schendzielorz, A. B., Melchionda, L., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.11.001 · Cited by 318 · see citing works
A reference human induced pluripotent stem cell line for large-scale collaborative studies
Pantazis, C. B., Yang, A., Lara, E., McDonough, J. A., Blauwendraat, C., Peng, L., Oguro, H., Kanaujiya, J., Zou, J., Sebesta, D., et al. (2022) · Cell Stem Cell · doi:10.1016/j.stem.2022.11.004 · Cited by 310 · see citing works
Atorino, L., Silvestri, L., Koppen, M., Cassina, L., Ballabio, A., Marconi, R., Langer, T., & Casari, G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200304112 · Cited by 283 · see citing works
SLC25A39 is necessary for mitochondrial glutathione import in mammalian cells
Wang, Y., Yen, F. S., Zhu, X. G., Timson, R. C., Weber, R. A., Xing, C., Liu, Y., Allwein, B., Luo, H., Yeh, H.-W., et al. (2021) · Nature · doi:10.1038/s41586-021-04025-w · Cited by 268 · see citing works
Requejo, R., Hurd, T. R., Costa, N. J., & Murphy, M. P. (2010) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07576.x · Cited by 231 · see citing works
Pierson, T. M., Adams, D. R., Bonn, F., Martinelli, P., Cherukuri, P. F., Teer, J. K., Hansen, N. F., Cruz, P., Mullikin, J. C., Blakesley, R. W., et al. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002325 · Cited by 226 · see citing works
Discovery of Genes Essential for Heme Biosynthesis through Large-Scale Gene Expression Analysis
Nilsson, R., Schultz, I. J., Pierce, E. L., Soltis, K. A., Naranuntarat, A., Ward, D. M., Baughman, J. M., Paradkar, P. N., Kingsley, P. D., Culotta, V., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.012 · Cited by 213 · see citing works
Crystal Structures of Nucleotide-Free and Glutathione-Bound Mitochondrial ABC Transporter Atm1
Srinivasan, V., Pierik, A. J., & Lill, R. (2014) · Science · doi:10.1126/science.1246729 · Cited by 212 · see citing works
Mitochondrial glutathione: Features, regulation and role in disease
Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.10.018 · Cited by 205 · see citing works
Koppen, M., Metodiev, M. D., Casari, G., Rugarli, E. I., & Langer, T. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01470-06 · Cited by 203 · see citing works
The SLC25 Carrier Family: Important Transport Proteins in Mitochondrial Physiology and Pathology
Kunji, E. R. S., King, M. S., Ruprecht, J. J., & Thangaratnarajah, C. (2020) · Physiology · doi:10.1152/physiol.00009.2020 · Cited by 181 · see citing works
Cellular pyrimidine imbalance triggers mitochondrial DNA–dependent innate immunity
Sprenger, H., MacVicar, T., Bahat, A., Fiedler, K. U., Hermans, S., Ehrentraut, D., Ried, K., Milenkovic, D., Bonekamp, N. A., Larsson, N., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00385-9 · Cited by 165 · see citing works
Principles and functions of metabolic compartmentalization
Bar-Peled, L., & Kory, N. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00645-2 · Cited by 157 · see citing works
Autoregulatory control of mitochondrial glutathione homeostasis
Liu, Y., Liu, S., Tomar, A., Yen, F. S., Ünlü, G., Ropek, N., Weber, R. A., Wang, Y., Khan, A., Gad, M., et al. (2023) · Science · doi:10.1126/science.adf4154 · Cited by 148 · see citing works
Luk, E., Carroll, M., Baker, M., & Culotta, V. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1632471100 · Cited by 146 · see citing works
Chen, W. W., Freinkman, E., & Sabatini, D. M. (2017) · Nature Protocols · doi:10.1038/nprot.2017.104 · Cited by 127 · see citing works
Peptide Level Turnover Measurements Enable the Study of Proteoform Dynamics
Zecha, J., Meng, C., Zolg, D. P., Samaras, P., Wilhelm, M., & Küster, B. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000583 · Cited by 123 · see citing works
Shi, X., Reinstadler, B. M., Shah, H., To, T., Byrne, K., Summer, L. C., Calvo, S. E., Goldberger, O., Doench, J. G., Mootha, V. K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30126-9 · Cited by 102 · see citing works
Self-citationIdentification of sixteen novel candidate genes for late onset Parkinson’s disease
Gialluisi, A., Reccia, M. G., Modugno, N., Nutile, T., Lombardi, A., Giovannantonio, L. G. D., Pietracupa, S., Ruggiero, D., Scala, S., Gambardella, S., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00455-2 · Cited by 99 · see citing works
Regulation of mitochondrial proteostasis by the proton gradient
Patrón, M., Tarasenko, D., Nolte, H., Kroczek, L., Ghosh, M., Ohba, Y., Lasarzewski, Y., Ahmadi, Z. A., Cabrera‐Orefice, A., Eiyama, A., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021110476 · Cited by 85 · see citing works
20,000 picometers under the OMM: diving into the vastness of mitochondrial metabolite transport
Cunningham, C. N., & Rutter, J. P. (2020) · EMBO Reports · doi:10.15252/embr.202050071 · Cited by 44 · see citing works
Magri, S., Fracasso, V., Plumari, M., Alfei, E., Ghezzi, D., Gellera, C., Rusmini, P., Poletti, A., Bella, D. D., Elia, A. E., et al. (2018) · Human Mutation · doi:10.1002/humu.23658 · Cited by 41 · see citing works
Byrne, K. L., Szeligowski, R. V., & Shen, H. (2023) · Biomolecules · doi:10.3390/biom13091314 · Cited by 12 · see citing works
Self-citationShi, X., Reinstadler, B. M., Shah, H., To, T., Byrne, K., Summer, L. C., Calvo, S. E., Goldberger, O., Doench, J. G., Mootha, V. K., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.22.461361 · Cited by 3 · see citing works
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Flagged first, then by citations
1 of the 48 references couldn’t be matched to a known paper.
Cited by
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Mitochondrial Glutathione in Cellular Redox Homeostasis and Disease Manifestation
Chen, T., Wang, H., Chang, C.-J., & Lee, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021314 · Cited by 241 · see citing works
Why cells need iron: a compendium of iron utilisation
Teh, M. R., Armitage, A. E., & Drakesmith, H. (2024) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2024.04.015 · Cited by 114 · see citing works
Solute carriers: The gatekeepers of metabolism
Khan, A., Liu, Y., Gad, M., Kenny, T. C., & Birsoy, K. (2025) · Cell · doi:10.1016/j.cell.2025.01.015 · Cited by 63 · see citing works
Pulling back the mitochondria’s iron curtain
David, S. B. Z., Shkuri, L., & Ast, T. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-024-00045-y · Cited by 46 · see citing works
Immunometabolism of ferroptosis in the tumor microenvironment
Lupica-Tondo, G. L., Arner, E. N., Mogilenko, D. A., & Voss, K. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1441338 · Cited by 26 · see citing works
SLC25A39 links mitochondrial GSH sensing with iron metabolism
Chen, X., & Gan, B. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.037 · Cited by 20 · see citing works
Miyahara, S., Ohuchi, M., Nomura, M., Hashimoto, E., Soga, T., Saito, R., Hayashi, K., Sato, T., Saito, M., Yamashita, Y., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107678 · Cited by 19 · see citing works
Aberrant Mitochondrial Metabolism in Alzheimer's Disease Links Energy Stress with Ferroptosis
Alves, F. M., Lane, D. J. R., Wahida, A., Jakaria, M., Kalinowski, P., Southon, A. G., Belaidi, A. A., Samperi‐Esteve, T., Nguyen, T. P. M., Peng, L., et al. (2025) · Advanced Science · doi:10.1002/advs.202504175 · Cited by 20 · see citing works
Requirements for the biogenesis of [2Fe-2S] proteins in the human and yeast cytosol
Braymer, J. J., Stehling, O., Stümpfig, M., Rösser, R., Spantgar, F., Blinn, C. M., Mühlenhoff, U., Pierik, A. J., & Lill, R. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2400740121 · Cited by 19 · see citing works
Dias, M. M., King, M. S., Shokry, E., Lilla, S., Paul, N. R., Thomason, P. A., Zanivan, S. R., Sumpton, D. P., Kunji, E. R. S., & MacVicar, T. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.08.018 · Cited by 18 · see citing works
Targeting mitochondria-regulated ferroptosis: A new frontier in Parkinson's disease therapy
Wang, W., Thomas, E. R., Xiao, R., Chen, T., Guo, Q., Liu, K., Yang, Y., & Li, X. (2025) · Neuropharmacology · doi:10.1016/j.neuropharm.2025.110439 · Cited by 16 · see citing works
Zhang, W., Ou, Z., Tang, T., Yang, T., Li, Y., Wu, H., Li, L., Liu, M., Niu, L., & Zhu, J. (2024) · Journal of Cancer · doi:10.7150/jca.98844 · Cited by 13 · see citing works
SLC25A38 is required for mitochondrial pyridoxal 5’-phosphate (PLP) accumulation
Pena, I. A., Shi, J. S., Chang, S. M., Yang, J., Block, S., Adelmann, C. H., Keys, H. R., Ge, P., Bathla, S., Witham, I. H., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56130-3 · Cited by 13 · see citing works
Yuan, Z., Liu, T., Jiang, P. X., Zhao, Y., Guo, R., Ye, X., He, Q., Wang, H., Xue, L., & Wang, J. (2025) · Science China Life Sciences · doi:10.1007/s11427-024-2938-3 · Cited by 11 · see citing works
The peculiar properties of mitochondrial carriers of the SLC25 family
Kunji, E. R. S., Mavridou, V., King, M. S., Cimadamore‐Werthein, C., Baron, S. J., Jones, S. A., King, A. C., Springett, R., Chand, D., Palmer, S. M., et al. (2025) · Biochemical Journal · doi:10.1042/bcj20253171 · Cited by 12 · see citing works
Fighting ischemia-reperfusion injury: Focusing on mitochondria-derived ferroptosis
Tian, L., Liu, Q., Guo, H. W., Zang, H., & Li, Y. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101974 · Cited by 11 · see citing works
Liu, R., Zhang, Z., Kyaw, A., Grabińska, K. A., Shah, H., & Shen, H. (2025) · Nature Metabolism · doi:10.1038/s42255-025-01358-y · Cited by 11 · see citing works
Self-citationTranscriptomic profile of premature ovarian insufficiency with RNA-sequencing
Wu, J., Feng, S., Luo, Y., Ning, Y., Qiu, P., Lin, Y., Ma, F., & Zhuo, Y. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1370772 · Cited by 9 · see citing works
Mitochondria as sensors of intracellular pathogens
Delgado, J. M., & Pernas, L. F. (2024) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2024.10.009 · Cited by 7 · see citing works
Ducamp, S., Wu, M., Putra, J., Campagna, D. R., Xiang, Y., Hong, V., Heeney, M. M., Dickey, A. K., Leaf, R. K., Fleming, M. D., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci181875 · Cited by 7 · see citing works
Wang, L., Li, W., Wu, X., Ouyang, Q., Sun, B., Luo, J., Guo, H., Yang, T., & Ma, Y. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06969-3 · Cited by 7 · see citing works
Torti, S. V., Tesfay, L., & Torti, F. M. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-92033-2_18 · Cited by 6 · see citing works
Mitochondrial glutathione transporter SLC25A40 regulates macrophage cytokine production
Yin, M., Pålsson‐McDermott, E. M., Henry, Ó. C., Ge, Z., Toller-Kawahisa, J. E., Min, Y., McGettrick, A. F., Gordon, A. L., Heffernan, S. B., Marrone, L., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-30333-6 · Cited by 6 · see citing works
Pham, T., Schelling, R. E., & Loh, K. H. (2025) · Advances in genetics · doi:10.1016/bs.adgen.2025.02.001 · Cited by 5 · see citing works
Wang, B., Han, X., Lin, X., Wang, J., You, C., Chen, K., Chen, Y., Meng, F., Jiang, H., Zheng, F., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64734-y · Cited by 4 · see citing works
D’Addabbo, P., Grassi, A., Luca, D., Scaglione, V., Francavilla, A. L., Todisco, S., Sgobba, M. N., Guerra, L., Volpicella, M., Beheshti, A., et al. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07505-z · Cited by 4 · see citing works
Glutathione-driven redox decisions in cell survival and death
Zhang, R., Kang, R., & Tang, D. (2026) · Vita · doi:10.15302/vita.2026.06.0040 · Cited by 4 · see citing works
Hu, W., Yang, J., Chen, Z., Li, Y., Luo, G., Hu, K., Lu, Z., Lv, X., Cao, Y., Yuan, H., et al. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-01081-7 · Cited by 3 · see citing works
SLC25A39 binds and modulates PRDX1 to suppress ROS-induced necroptosis in hepatocellular carcinoma
Liu, W., Kuang, T., Dong, K., Li, M., Deng, W., & Yu, J. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116246 · Cited by 3 · see citing works
Cui, W., Xiao, H., Wen, X., Li, C., Bao, S., Zeng, J., Li, Y., Qiao, Y., Wang, K., Wang, H., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2514681123 · Cited by 3 · see citing works
Xu, Y., Yang, Z., Wang, T., Hu, L., Jiao, S., Zhou, J., Dai, T., Feng, Z., Li, S., & Meng, Q. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e35774 · Cited by 3 · see citing works
Yuan, M., Du, M., Yu, J., Wang, J., Xia, T., Shen, Q., Wang, C., & Li, R. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00829-0 · Cited by 2 · see citing works
Chen, Y., Zhang, B., Wei, Y., Dai, Y., Zhang, B., Li, J., Wu, K., Sun, N., & Shao, C. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104131 · Cited by 2 · see citing works
Qiu, E., Lv, G., Hou, J., Li, Z., & Wang, G. (2026) · iScience · doi:10.1016/j.isci.2026.116449 · Cited by 2 · see citing works
Mitochondria setting the stage for ferroptosis
Ahola, S. (2026) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2026.06.006 · Cited by 2 · see citing works
Tan, S., Dengler, A., Darawsheh, R. Z., & Kory, N. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.12.593764 · Cited by 2 · see citing works
Control of mitochondrial glutathione homeostasis by SLC25A39
Liu, J., & Zuo, S. (2024) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2024072 · Cited by 1 · see citing works
Toxoplasma survives the loss of key enzymes of peroxide and glutathione metabolism
Guo, Q., Pan, J., Guo, X., Zhao, M., Du, H., Wang, M., Deponte, M., Zhong, X., Xiao, L., Feng, Y., et al. (2025) · The FASEB Journal · doi:10.1096/fj.202402341r · Cited by 1 · see citing works
Hashimoto, E., Ohuchi, M., Nomura, M., Miyahara, S., Hayashi, K., Saito, M., Yamashita, Y., Shimada, M., Yamada, H., & Tanuma, N. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113200 · Cited by 1 · see citing works
AFG3L2-mediated proteolysis restricts mitochondrial biogenesis and gene expression in hypoxiaPreprint
Chandragiri, S., Grotehans, N., Lasarzewski, Y., Patrón, M., MacVicar, T., Ohba, Y., Hermans, S., Rugarli, E. I., Nolte, H., & Langer, T. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.27.615438 · Cited by 1 · see citing works
Biezeman, H., Nubiè, M., & Oburoglu, L. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107815 · Cited by 1 · see citing works
Kelly, B., Wu, C.-H., Eskut, K. I., McCauley, E., Dhungel, S., Pavlecic, S., Bieghler, G., Perovanović, J., Tantin, D. R., Famulski, J. K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.02.680066
Zhang, G., Huang, Y., Li, Z., Ma, P., Sun, X., Zhou, L., Liu, Z., & Wu, B. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5660883
Mitochondrial Dysfunction, Transfer, and Therapeutic Strategies in Neurological Disorders
Ling, L., Chen, D., Wang, C., & Dang, R. (2026) · Neuropharmacology and Therapy · doi:10.15212/npt-2025-0020
Zhang, K., Zhang, X., Huang, C., Yang, J., Dong, L., Chen, X., Xun, C., & Guo, Y. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.04.133
Iron and immunometabolism: Perspectives from the lung
Faherty, L., Jordan, R., & Cloonan, S. M. (2026) · Current Opinion in Endocrine and Metabolic Research · doi:10.1016/j.coemr.2026.100613
Loss of Function of AFG3L2 Leading to Developmental and Epileptic Encephalopathy
Pan, Z., Yang, L., Tang, H., Chen, C., Yang, Q., 巫腾辉, He, F. P., Zhang, Z., Liu, F., & Peng, J. (2026) · CNS Neuroscience & Therapeutics · doi:10.1002/cns.71013
Li, Z., Qiao, W., Fan, B., Qiu, F., & Su, W. (2026) · iScience · doi:10.1016/j.isci.2026.117098
Pan, G., Zhang, S.-P., Wang, X., Qu, Y., Liu, X., Yan, Y., Li, T., & Dong, Z. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104342
Sato, T., Yamaguchi, K., Wada, T., Shimba, S., Abe, T., Tanigawa, Y., & Oishi, K. (2026) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2026.117997
Badiu, F., & SLEVIN, M. A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27198642
Geertsema, S., Loveikyte, R., de Jong, S., Bulthuis, M. L. C., Reinders-Luinge, M., van Goor, H., Faber, K. N., Bourgonje, A. R., & Dijkstra, G. D. H. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1908844
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Tian, T., Jin, Y., Cui, P., & Lan, S. (2026) · Medical Oncology · doi:10.1007/s12032-026-03466-5
Mitochondrial dysfunction in Parkinson's disease and aging
Lu, X., Huang, Z., & Ying, Z. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1914316
- Authors
- Shi, X., DeCiucis, M., Grabinska, K. A., Kanyo, J., Liu, A., Lam, T. T., & Shen, H.
- Affiliations
- Yale University (US)
- Corresponding author
- Shen, Hongying
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2024-02
- Volume
- 84
- Issue
- 4
- Pages
- 802-810.e6
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC10922821
- OpenAlex
- W4390350694
- Cited by
- 54
- References
- 48
- Citations by year
- 2026: 18 · 2025: 21 · 2024: 15
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 380 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (S10OD018034, S10OD019967, S10OD02365101A1)
- National Institute of General Medical Sciences (R35GM150619)
- Office of the Director
- Rita Allen Foundation
- Yale University
- Yale School of Medicine
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- AFG3L2, iron homeostasis, iron-sulfur clusters, protein degradation, protein quality control, metabolic compartmentation, neurodegeneration
- MeSH terms
- ATPases Associated with Diverse Cellular Activities, Animals, Glutathione, Homeostasis, Humans, Iron, Mammals, Mitochondria, Mitochondrial Proteins, Mitochondrial Membrane Transport Proteins, ATP-Dependent Proteases
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