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SLC7A11 is an unconventional H+ transporter in lysosomes

Zhou, Nan, Chen, Jingzhi, Hu, Meiqin, Wen, Na, Cai, Weijie, Li, Ping, Zhao, Liding, Meng, Yaping, Zhao, Dongdong, Yang, Xiaotong, Liu, Siyu, Huang, Fangqian, Zhao, Cheng, Feng, Xinghua, Jiang, Zikai, Xie, Enjun, Pan, Hongxu, Cen, Zhidong, Chen, Xinhui, Luo, Wei, Tang, Beisha, Min, Junxia, Wang, Fudi, Yang, Junsheng, Xu, Haoxing·2025·Cell

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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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Research works printed but not linked: 81

  1. 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
  2. Hu, 2022, Lysosomal solute and water transport, J. Cell Biol., 221, 10.1083/jcb.202109133 · DOI
  3. Hu, 2024, The Ion Channels of Endomembranes, Physiol. Rev., 104, 1335, 10.1152/physrev.00025.2023 · DOI
  4. Xu, 2015, Lysosomal physiology, Annu. Rev. Physiol., 77, 57, 10.1146/annurev-physiol-021014-071649 · DOI
  5. 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
  6. Freeman, 2023, Determinants, maintenance, and function of organellar pH, Physiol. Rev., 103, 515, 10.1152/physrev.00009.2022 · DOI
  7. 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
  8. 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
  9. 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
  10. Bourdenx, 2016, Nanoparticles restore lysosomal acidification defects: Implications for Parkinson and other lysosomal-related diseases, Autophagy, 12, 472, 10.1080/15548627.2015.1136769 · DOI
  11. Bonam, 2019, Lysosomes as a therapeutic target, Nat. Rev. Drug Discov., 18, 923, 10.1038/s41573-019-0036-1 · DOI
  12. 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
  13. Ishida, 2013, A model of lysosomal pH regulation, J. Gen. Physiol., 141, 705, 10.1085/jgp.201210930 · DOI
  14. 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
  15. 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
  16. Kosmidis, 2022, Regulation of the mammalian-brain V-ATPase through ultraslow mode-switching, Nature, 611, 827, 10.1038/s41586-022-05472-9 · DOI
  17. 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
  18. Zheng, 2022, pH regulates potassium conductance and drives a constitutive proton current in human TMEM175, Sci. Adv., 8, 10.1126/sciadv.abm1568 · DOI
  19. Hu, 2023, The Acid Gate in the Lysosome, Autophagy, 19, 1368, 10.1080/15548627.2022.2125629 · DOI
  20. Steinberg, 2010, A cation counterflux supports lysosomal acidification, J. Cell Biol., 189, 1171, 10.1083/jcb.200911083 · DOI
  21. 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
  22. Wang, 2015, Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1, Science, 347, 188, 10.1126/science.1257132 · DOI
  23. Lloyd, 1971, A study of permeability of lysosomes to amino acids and small peptides, Biochem. J., 121, 245, 10.1042/bj1210245 · DOI
  24. 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
  25. Stockwell, 2022, Ferroptosis turns 10: Emerging mechanisms, physiological functions, and therapeutic applications, Cell, 185, 2401, 10.1016/j.cell.2022.06.003 · DOI
  26. Jiang, 2021, Ferroptosis: mechanisms, biology and role in disease, Nat. Rev. Mol. Cell Biol., 22, 266, 10.1038/s41580-020-00324-8 · DOI
  27. 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
  28. 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
  29. 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
  30. 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
  31. 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
  32. DiCiccio, 2011, Lysosomal pH and analysis of the counter ion pathways that support acidification, J. Gen. Physiol., 137, 385, 10.1085/jgp.201110596 · DOI
  33. 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
  34. 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
  35. Jurgeit, 2012, Niclosamide is a proton carrier and targets acidic endosomes with broad antiviral effects, PLoS Pathog., 8, 10.1371/journal.ppat.1002976 · DOI
  36. Dixon, 2012, Ferroptosis: an iron-dependent form of nonapoptotic cell death, Cell, 149, 1060, 10.1016/j.cell.2012.03.042 · DOI · Paper page
  37. 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
  38. 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
  39. Vasanthakumar, 2020, Structure and Roles of V-type ATPases, Trends Biochem. Sci., 45, 295, 10.1016/j.tibs.2019.12.007 · DOI
  40. 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
  41. Maschalidi, 2022, Targeting SLC7A11 improves efferocytosis by dendritic cells and wound healing in diabetes, Nature, 606, 776, 10.1038/s41586-022-04754-6 · DOI
  42. 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
  43. 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
  44. 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
  45. Dong, 2008, The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel, Nature, 455, 992, 10.1038/nature07311 · DOI
  46. 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
  47. Braulke, 2009, Sorting of lysosomal proteins, Biochim. Biophys. Acta, 1793, 605, 10.1016/j.bbamcr.2008.10.016 · DOI · Paper page
  48. 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
  49. 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
  50. 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
  51. Yang, 2014, Regulation of ferroptotic cancer cell death by GPX4, Cell, 156, 317, 10.1016/j.cell.2013.12.010 · DOI · Paper page
  52. Bannai, 1984, Amino acid transport systems, Nature, 311
  53. Liu, 2012, LAAT-1 is the lysosomal lysine/arginine transporter that maintains amino acid homeostasis, Science, 337, 351, 10.1126/science.1220281 · DOI
  54. 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
  55. Adelmann, 2020, MFSD12 mediates the import of cysteine into melanosomes and lysosomes, Nature, 588, 699, 10.1038/s41586-020-2937-x · DOI
  56. Fiore, 2022, Kynurenine importation by SLC7A11 propagates anti-ferroptotic signaling, Mol. Cell, 82, 920, 10.1016/j.molcel.2022.02.007 · DOI
  57. Schnell, 1999, Reduction of lipofuscin-like autofluorescence in fluorescently labeled tissue, J. Histochem. Cytochem., 47, 719, 10.1177/002215549904700601 · DOI
  58. Briozzo, 1988, In vitro degradation of extracellular matrix with Mr 52,000 cathepsin D secreted by breast cancer cells, Cancer Res., 48, 3688
  59. Li, 2019, Lysosomal Ion Channels as Decoders of Cellular Signals, Trends Biochem. Sci., 44, 110, 10.1016/j.tibs.2018.10.006 · DOI
  60. Platt, 2018, Lysosomal storage diseases, Nat. Rev. Dis. Primers, 4
  61. 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
  62. Rizzollo, 2021, The lysosome as a master regulator of iron metabolism, Trends Biochem. Sci., 46, 960, 10.1016/j.tibs.2021.07.003 · DOI
  63. Armenta, 2022, Ferroptosis inhibition by lysosome-dependent catabolism of extracellular protein, Cell Chem. Biol., 29, 1588, 10.1016/j.chembiol.2022.10.006 · DOI
  64. Liu, 2021, NUPR1 is a critical repressor of ferroptosis, Nat. Commun., 12
  65. 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
  66. Liu, 2022, DCN released from ferroptotic cells ignites AGER-dependent immune responses, Autophagy, 18, 2036, 10.1080/15548627.2021.2008692 · DOI
  67. 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
  68. 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
  69. Yoo, 2011, MicroRNA-mediated conversion of human fibroblasts to neurons, Nature, 476, 228, 10.1038/nature10323 · DOI · Paper page
  70. 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
  71. McGlinchey, 2015, Cysteine cathepsins are essential in lysosomal degradation of alpha-synuclein, Proc. Natl. Acad. Sci. USA, 112, 9322, 10.1073/pnas.1500937112 · DOI
  72. Luk, 2012, Pathological alpha-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice, Science, 338, 949, 10.1126/science.1227157 · DOI · Paper page
  73. Levin-Konigsberg, 2023, SLC12A9 is a lysosome-detoxifying ammonium - chloride co-transporter, bioRxiv
  74. 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
  75. Li, 2022, Phospholipid peroxidation inhibits autophagy via stimulating the delipidation of oxidized LC3-PE, Redox Biol., 55, 10.1016/j.redox.2022.102421 · DOI
  76. Li, 2024, 7-Dehydrocholesterol dictates ferroptosis sensitivity, Nature, 626, 411, 10.1038/s41586-023-06983-9 · DOI
  77. Wang, 2017, Characterization of ferroptosis in murine models of hemochromatosis, Hepatology, 66, 449, 10.1002/hep.29117 · DOI
  78. Ran, 2013, Genome engineering using the CRISPR-Cas9 system, Nat. Protoc., 8, 2281, 10.1038/nprot.2013.143 · DOI · Paper page
  79. Shin, 2017, The glutamate/cystine xCT antiporter antagonizes glutamine metabolism and reduces nutrient flexibility, Nat. Commun., 8, 10.1038/ncomms15074 · DOI
  80. 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
  81. 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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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
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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