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SLC7A11 is an unconventional H+ transporter in lysosomes
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Increased SLC7A11 lysosomal levels upon SNX3-Retromer deficiency may contribute to the lysosomal acidification defects observed upon loss of VPS35 expression.
“Increased SLC7A11 lysosomal levels upon SNX3-Retromer deficiency may therefore contribute to the lysosomal acidification defects observed upon loss of VPS35 expression [131, 132].”
From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [132]
The passage headed “Increasing SLC7A11 expression promotes lysosomal H+ efflux in cells” reports that SLC7A11 overexpression reduced lysosomal acidity, supporting the proposed direction of its effect. Our copy does not establish that SNX3-Retromer deficiency increases lysosomal SLC7A11 or that SLC7A11 contributes to the acidification defect upon VPS35 loss; searches for SNX3 and VPS35 found no such passage. Page numbers were unavailable in the indexed copy. (LLM, conf=0.85)
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MDS clinical diagnostic criteria for Parkinson’s disease
Postuma, R. B., Berg, D., Stern, M., Poewe, W., Olanow, C. W., Oertel, W., Obeso, J., Marek, K., Litvan, I., Lang, A. E., et al. (2015) · Movement Disorders · doi:10.1002/mds.26424 · Cited by 7,653
Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
Friedmann Angeli, J. P., Schneider, M., Proneth, B., Tyurina, Y. Y., Tyurin, V. A., Hammond, V. J., Herbach, N., Aichler, M., Walch, A., Eggenhofer, E., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3064 · Cited by 3,732
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897
Self-citationLysosomal acidification mechanisms
Mindell, J. A. (2012) · Annual Review of Physiology · doi:10.1146/annurev-physiol-012110-142317 · Cited by 1,258
Gout, P., Buckley, A., Simms, C., & Bruchovsky, N. (2001) · Leukemia · doi:10.1038/sj.leu.2402238 · Cited by 640
The position of lysosomes within the cell determines their luminal pH
Johnson, D. E., Ostrowski, P., Jaumouillé, V., & Grinstein, S. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201507112 · Cited by 590
Redox imbalance in cystine/glutamate transporter-deficient mice
Sato, H., Shiiya, A., Kimata, M., Maebara, K., Tamba, M., Sakakura, Y., Makino, N., Sugiyama, F., Yagami, K.-I., Moriguchi, T., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506439200 · Cited by 422
An essential role for functional lysosomes in ferroptosis of cancer cells
Torii, S., Shintoku, R., Kubota, C., Yaegashi, M., Torii, R., Sasaki, M., Suzuki, T., Mori, M., Yoshimoto, Y., Takeuchi, T., et al. (2016) · Biochemical Journal · doi:10.1042/bj20150658 · Cited by 349
Flagged first, then by citations
Research works printed but not linked: 81
- Kolter, 2005, Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids, Annu. Rev. Cell Dev. Biol., 21, 81, 10.1146/annurev.cellbio.21.122303.120013 · DOI · Paper page
- Hu, 2022, Lysosomal solute and water transport, J. Cell Biol., 221, 10.1083/jcb.202109133 · DOI
- Hu, 2024, The Ion Channels of Endomembranes, Physiol. Rev., 104, 1335, 10.1152/physrev.00025.2023 · DOI
- Xu, 2015, Lysosomal physiology, Annu. Rev. Physiol., 77, 57, 10.1146/annurev-physiol-021014-071649 · DOI
- Ballabio, 2020, Lysosomes as dynamic regulators of cell and organismal homeostasis, Nat. Rev. Mol. Cell Biol., 21, 101, 10.1038/s41580-019-0185-4 · DOI · Paper page
- Freeman, 2023, Determinants, maintenance, and function of organellar pH, Physiol. Rev., 103, 515, 10.1152/physrev.00009.2022 · DOI
- Holopainen, 2001, Elevated lysosomal pH in neuronal ceroid lipofuscinoses (NCLs), Eur. J. Biochem., 268, 5851, 10.1046/j.0014-2956.2001.02530.x · DOI · Paper page
- Lee, 2010, Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations, Cell, 141, 1146, 10.1016/j.cell.2010.05.008 · DOI · Paper page
- Nicoli, 2019, Lysosomal Storage and Albinism Due to Effects of a De Novo CLCN7 Variant on Lysosomal Acidification, Am. J. Hum. Genet., 104, 1127, 10.1016/j.ajhg.2019.04.008 · DOI
- Bourdenx, 2016, Nanoparticles restore lysosomal acidification defects: Implications for Parkinson and other lysosomal-related diseases, Autophagy, 12, 472, 10.1080/15548627.2015.1136769 · DOI
- Bonam, 2019, Lysosomes as a therapeutic target, Nat. Rev. Drug Discov., 18, 923, 10.1038/s41573-019-0036-1 · DOI
- Ratto, 2022, Direct control of lysosomal catabolic activity by mTORC1 through regulation of V-ATPase assembly, Nat. Commun., 13, 10.1038/s41467-022-32515-6 · DOI
- Ishida, 2013, A model of lysosomal pH regulation, J. Gen. Physiol., 141, 705, 10.1085/jgp.201210930 · DOI
- Zhou, 2013, Activation of lysosomal function in the course of autophagy via mTORC1 suppression and autophagosome-lysosome fusion, Cell Res., 23, 508, 10.1038/cr.2013.11 · DOI
- Maxson, 2014, The vacuolar-type H(+)-ATPase at a glance – more than a proton pump, J. Cell Sci., 127, 4987, 10.1242/jcs.158550 · DOI
- Kosmidis, 2022, Regulation of the mammalian-brain V-ATPase through ultraslow mode-switching, Nature, 611, 827, 10.1038/s41586-022-05472-9 · DOI
- Hu, 2022, Parkinson's disease-risk protein TMEM175 is a proton-activated proton channel in lysosomes, Cell, 185, 2292, 10.1016/j.cell.2022.05.021 · DOI · Paper page
- Zheng, 2022, pH regulates potassium conductance and drives a constitutive proton current in human TMEM175, Sci. Adv., 8, 10.1126/sciadv.abm1568 · DOI
- Hu, 2023, The Acid Gate in the Lysosome, Autophagy, 19, 1368, 10.1080/15548627.2022.2125629 · DOI
- Steinberg, 2010, A cation counterflux supports lysosomal acidification, J. Cell Biol., 189, 1171, 10.1083/jcb.200911083 · DOI
- Abu-Remaileh, 2017, Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes, Science, 358, 807, 10.1126/science.aan6298 · DOI
- Wang, 2015, Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1, Science, 347, 188, 10.1126/science.1257132 · DOI
- Lloyd, 1971, A study of permeability of lysosomes to amino acids and small peptides, Biochem. J., 121, 245, 10.1042/bj1210245 · DOI
- Sato, 1999, Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins, J. Biol. Chem., 274, 11455, 10.1074/jbc.274.17.11455 · DOI
- Stockwell, 2022, Ferroptosis turns 10: Emerging mechanisms, physiological functions, and therapeutic applications, Cell, 185, 2401, 10.1016/j.cell.2022.06.003 · DOI
- Jiang, 2021, Ferroptosis: mechanisms, biology and role in disease, Nat. Rev. Mol. Cell Biol., 22, 266, 10.1038/s41580-020-00324-8 · DOI
- Bannai, 1981, Role of proton dissociation in the transport of cystine and glutamate in human diploid fibroblasts in culture, J. Biol. Chem., 256, 5770, 10.1016/S0021-9258(19)69273-2 · DOI
- Bowman, 1988, Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells, Proc. Natl. Acad. Sci. USA, 85, 7972, 10.1073/pnas.85.21.7972 · DOI
- Sleat, 2019, Analysis of Brain and Cerebrospinal Fluid from Mouse Models of the Three Major Forms of Neuronal Ceroid Lipofuscinosis Reveals Changes in the Lysosomal Proteome, Mol. Cell. Proteomics, 18, 2244, 10.1074/mcp.RA119.001587 · DOI
- Tharkeshwar, 2017, A novel approach to analyze lysosomal dysfunctions through subcellular proteomics and lipidomics: the case of NPC1 deficiency, Sci. Rep., 7, 10.1038/srep41408 · DOI
- Eapen, 2021, Quantitative proteomics reveals the selectivity of ubiquitin-binding autophagy receptors in the turnover of damaged lysosomes by lysophagy, eLife, 10, 10.7554/eLife.72328 · DOI
- DiCiccio, 2011, Lysosomal pH and analysis of the counter ion pathways that support acidification, J. Gen. Physiol., 137, 385, 10.1085/jgp.201110596 · DOI
- Bassi, 2001, Identification and characterisation of human xCT that co-expresses, with 4F2 heavy chain, the amino acid transport activity system xc-, Pflugers Arch., 442, 286, 10.1007/s004240100537 · DOI
- Geng, 2020, DRAM1 plays a tumor suppressor role in NSCLC cells by promoting lysosomal degradation of EGFR, Cell Death Dis., 11, 10.1038/s41419-020-02979-9 · DOI
- Jurgeit, 2012, Niclosamide is a proton carrier and targets acidic endosomes with broad antiviral effects, PLoS Pathog., 8, 10.1371/journal.ppat.1002976 · DOI
- Dixon, 2012, Ferroptosis: an iron-dependent form of nonapoptotic cell death, Cell, 149, 1060, 10.1016/j.cell.2012.03.042 · DOI · Paper page
- Yan, 2022, The structure of erastin-bound xCT-4F2hc complex reveals molecular mechanisms underlying erastin-induced ferroptosis, Cell Res., 32, 687, 10.1038/s41422-022-00642-w · DOI
- Zheng, 2021, Sorafenib fails to trigger ferroptosis across a wide range of cancer cell lines, Cell Death Dis., 12, 10.1038/s41419-021-03998-w · DOI
- Vasanthakumar, 2020, Structure and Roles of V-type ATPases, Trends Biochem. Sci., 45, 295, 10.1016/j.tibs.2019.12.007 · DOI
- Zhang, 2019, Imidazole Ketone Erastin Induces Ferroptosis and Slows Tumor Growth in a Mouse Lymphoma Model, Cell Chem. Biol., 26, 623, 10.1016/j.chembiol.2019.01.008 · DOI
- Maschalidi, 2022, Targeting SLC7A11 improves efferocytosis by dendritic cells and wound healing in diabetes, Nature, 606, 776, 10.1038/s41586-022-04754-6 · DOI
- Webb, 2021, pHLARE: a new biosensor reveals decreased lysosome pH in cancer cells, Mol. Biol. Cell, 32, 131, 10.1091/mbc.E20-06-0383 · DOI
- Maxson, 2022, Detection and quantification of the vacuolar H+ATPase using the Legionella effector protein SidK, J. Cell Biol., 221, 10.1083/jcb.202107174 · DOI
- Huynh, 2005, The small chemical vacuolin-1 alters the morphology of lysosomes without inhibiting Ca2+-regulated exocytosis, EMBO Rep., 6, 843, 10.1038/sj.embor.7400495 · DOI
- Dong, 2008, The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel, Nature, 455, 992, 10.1038/nature07311 · DOI
- Swanda, 2023, Lysosomal cystine governs ferroptosis sensitivity in cancer via cysteine stress response, Mol. Cell, 83, 3347, 10.1016/j.molcel.2023.08.004 · DOI
- Braulke, 2009, Sorting of lysosomal proteins, Biochim. Biophys. Acta, 1793, 605, 10.1016/j.bbamcr.2008.10.016 · DOI · Paper page
- Parker, 2021, Molecular basis for redox control by the human cystine/glutamate antiporter system xc, Nat. Commun., 12, 10.1038/s41467-021-27414-1 · DOI · Paper page
- Lim, 2019, Cystine/glutamate antiporter xCT (SLC7A11) facilitates oncogenic RAS transformation by preserving intracellular redox balance, Proc. Natl. Acad. Sci. USA, 116, 9433, 10.1073/pnas.1821323116 · DOI
- Ishii, 1981, Mechanism of growth stimulation of L1210 cells by 2-mercaptoethanol in vitro. Role of the mixed disulfide of 2-mercaptoethanol and cysteine, J. Biol. Chem., 256, 12387, 10.1016/S0021-9258(18)43284-X · DOI
- Yang, 2014, Regulation of ferroptotic cancer cell death by GPX4, Cell, 156, 317, 10.1016/j.cell.2013.12.010 · DOI · Paper page
- Bannai, 1984, Amino acid transport systems, Nature, 311
- Liu, 2012, LAAT-1 is the lysosomal lysine/arginine transporter that maintains amino acid homeostasis, Science, 337, 351, 10.1126/science.1220281 · DOI
- Kalatzis, 2001, Cystinosin, the protein defective in cystinosis, is a H(+)-driven lysosomal cystine transporter, EMBO J., 20, 5940, 10.1093/emboj/20.21.5940 · DOI
- Adelmann, 2020, MFSD12 mediates the import of cysteine into melanosomes and lysosomes, Nature, 588, 699, 10.1038/s41586-020-2937-x · DOI
- Fiore, 2022, Kynurenine importation by SLC7A11 propagates anti-ferroptotic signaling, Mol. Cell, 82, 920, 10.1016/j.molcel.2022.02.007 · DOI
- Schnell, 1999, Reduction of lipofuscin-like autofluorescence in fluorescently labeled tissue, J. Histochem. Cytochem., 47, 719, 10.1177/002215549904700601 · DOI
- Briozzo, 1988, In vitro degradation of extracellular matrix with Mr 52,000 cathepsin D secreted by breast cancer cells, Cancer Res., 48, 3688
- Li, 2019, Lysosomal Ion Channels as Decoders of Cellular Signals, Trends Biochem. Sci., 44, 110, 10.1016/j.tibs.2018.10.006 · DOI
- Platt, 2018, Lysosomal storage diseases, Nat. Rev. Dis. Primers, 4
- Mazzulli, 2011, Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies, Cell, 146, 37, 10.1016/j.cell.2011.06.001 · DOI · Paper page
- Rizzollo, 2021, The lysosome as a master regulator of iron metabolism, Trends Biochem. Sci., 46, 960, 10.1016/j.tibs.2021.07.003 · DOI
- Armenta, 2022, Ferroptosis inhibition by lysosome-dependent catabolism of extracellular protein, Cell Chem. Biol., 29, 1588, 10.1016/j.chembiol.2022.10.006 · DOI
- Liu, 2021, NUPR1 is a critical repressor of ferroptosis, Nat. Commun., 12
- Li, 2020, LRRC8 family proteins within lysosomes regulate cellular osmoregulation and enhance cell survival to multiple physiological stresses, Proc. Natl. Acad. Sci. USA, 117, 29155, 10.1073/pnas.2016539117 · DOI
- Liu, 2022, DCN released from ferroptotic cells ignites AGER-dependent immune responses, Autophagy, 18, 2036, 10.1080/15548627.2021.2008692 · DOI
- Vallerga, 2020, Analysis of DNA methylation associates the cystine-glutamate antiporter SLC7A11 with risk of Parkinson's disease, Nat. Commun., 11, 10.1038/s41467-020-15065-7 · DOI
- Wang, 2022, Ferroptosis in Parkinson's disease: glia-neuron crosstalk, Trends Mol. Med., 28, 258, 10.1016/j.molmed.2022.02.003 · DOI · Paper page
- Yoo, 2011, MicroRNA-mediated conversion of human fibroblasts to neurons, Nature, 476, 228, 10.1038/nature10323 · DOI · Paper page
- Kriks, 2011, Dopamine neurons derived from human ES cells efficiently engraft in animal models of Parkinson's disease, Nature, 480, 547, 10.1038/nature10648 · DOI
- McGlinchey, 2015, Cysteine cathepsins are essential in lysosomal degradation of alpha-synuclein, Proc. Natl. Acad. Sci. USA, 112, 9322, 10.1073/pnas.1500937112 · DOI
- Luk, 2012, Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice, Science, 338, 949, 10.1126/science.1227157 · DOI · Paper page
- Levin-Konigsberg, 2023, SLC12A9 is a lysosome-detoxifying ammonium - chloride co-transporter, bioRxiv
- Weber, 2020, Maintaining Iron Homeostasis Is the Key Role of Lysosomal Acidity for Cell Proliferation, Mol. Cell, 77, 645, 10.1016/j.molcel.2020.01.003 · DOI · Paper page
- Li, 2022, Phospholipid peroxidation inhibits autophagy via stimulating the delipidation of oxidized LC3-PE, Redox Biol., 55, 10.1016/j.redox.2022.102421 · DOI
- Li, 2024, 7-Dehydrocholesterol dictates ferroptosis sensitivity, Nature, 626, 411, 10.1038/s41586-023-06983-9 · DOI
- Wang, 2017, Characterization of ferroptosis in murine models of hemochromatosis, Hepatology, 66, 449, 10.1002/hep.29117 · DOI
- Ran, 2013, Genome engineering using the CRISPR-Cas9 system, Nat. Protoc., 8, 2281, 10.1038/nprot.2013.143 · DOI · Paper page
- Shin, 2017, The glutamate/cystine xCT antiporter antagonizes glutamine metabolism and reduces nutrient flexibility, Nat. Commun., 8, 10.1038/ncomms15074 · DOI
- Zhong, 2018, Prion-like protein aggregates exploit the RHO GTPase to cofilin-1 signaling pathway to enter cells, EMBO J., 37, 10.15252/embj.201797822 · DOI
- Ye, 2023, TRPM2 as a conserved gatekeeper determines the vulnerability of DA neurons by mediating ROS sensing and calcium dyshomeostasis, Prog. Neurobiol., 231, 10.1016/j.pneurobio.2023.102530 · DOI
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Jones, E., Adams, H., Chen, K.-E., Maroof, F., Ibbotson, T. M., Nakamura, Y., Banks, P. J., Healy, M. D., Lewis, P. A., Heesom, K. J., et al. (2026) · doi:10.64898/2026.05.14.724903
Metadata
- Authors
- Zhou, N., Chen, J., Hu, M., Wen, N., Cai, W., Li, P., Zhao, L., Meng, Y., Zhao, D., Yang, X., Liu, S., Huang, F., Zhao, C., Feng, X., Jiang, Z., Xie, E., Pan, H., Cen, Z., Chen, X., Luo, W., Tang, B., Min, J., Wang, F., Yang, J., & Xu, H.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2025-06
- Volume
- 188
- Issue
- 13
- Pages
- 3441-3458.e25
- ISSN
- 0092-8674
- Cited by
- 105
- References
- 8
- Language
- en
- Licence
- Funders
- National Natural Science Foundation of China (31930057, 32421001, 31970689, 32330047, 92354306)
- National Key Research and Development Program of China
- Innovative Research Group Project of the National Natural Science Foundation of China
- Key Technologies Research and Development Program (2022YFE0210100)
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