Cryo-EM structure of the human Asc-1 transporter complex
Open accessAbstract
The Alanine-Serine-Cysteine transporter 1 (Asc-1 or SLC7A10) forms a crucial heterodimeric transporter complex with 4F2hc (SLC3A2) through a covalent disulfide bridge. This complex enables the sodium-independent transport of small neutral amino acids, including L-Alanine (L-Ala), Glycine (Gly), and D-Serine (D-Ser), within the central nervous system (CNS). D-Ser and Gly are two key endogenous glutamate co-agonists that activate N-methyl-d-aspartate (NMDA) receptors by binding to the allosteric site. Mice deficient in Asc-1 display severe symptoms such as tremors, ataxia, and seizures, leading to early postnatal death. Despite its physiological importance, the functional mechanism of the Asc-1-4F2hc complex has remained elusive. Here, we present cryo-electron microscopy (cryo-EM) structures of the human Asc-1-4F2hc complex in its apo state, D-Ser bound state, and L-Ala bound state, resolved at 3.6 Å, 3.5 Å, and 3.4 Å, respectively. Through detailed structural analysis and transport assays, we uncover a comprehensive alternating access mechanism that underlies conformational changes in the complex. In summary, our findings reveal the architecture of the Asc-1 and 4F2hc complex and provide valuable insights into substrate recognition and the functional cycle of this essential transporter complex.
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SLC7A10 (also known as Asc-1) is a sodium-independent neutral amino acid transporter in neurons and astrocytes.
“SLC7A10 (also known as Asc-1) is a sodium-independent neutral amino acid transporter in neurons and astrocytes [60].”
From CI-994 is a dual modulator of class I HDACs and Wnt/β-catenin signaling for the treatment of Alzheimer's disease (2026) · cites this paper as [60]
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Cites
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · see citing works
MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works
Gctf: Real-time CTF determination and correction
Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,372 · see citing works
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416 · see citing works
Kanai, Y., Segawa, H., Miyamoto, K., Uchino, H., Takeda, E., & Endou, H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.37.23629 · Cited by 1,109 · see citing works
Chen, S., McMullan, G., Faruqi, A. R., Murshudov, G. N., Short, J. M., Scheres, S. H. W., & Henderson, R. A. (2013) · Ultramicroscopy · doi:10.1016/j.ultramic.2013.06.004 · Cited by 1,005 · see citing works
Flexible Fitting of Atomic Structures into Electron Microscopy Maps Using Molecular Dynamics
Trabuco, L. G., Villa, E., Mitra, K., Frank, J., & Schulten, K. J. (2008) · Structure · doi:10.1016/j.str.2008.03.005 · Cited by 866 · see citing works
Grant, T. S., & Grigorieff, N. (2015) · eLife · doi:10.7554/elife.06980 · Cited by 840 · see citing works
Yanagida, O., Kanai, Y., Chairoungdua, A., Kim, D. K., Segawa, H., Nii, T., Cha, S. H., Matsuo, H., Fukushima, J.-I., Fukasawa, Y., et al. (2001) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(01)00384-4 · Cited by 746 · see citing works
CATs and HATs: the SLC7 family of amino acid transporters
Verrey, F., Closs, E. I., Wagner, C. A., Palacı́n, M., Endou, H., & Kanai, Y. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1086-z · Cited by 709 · see citing works
Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000131 · Cited by 686 · see citing works
The SLC3 and SLC7 families of amino acid transporters
Fotiadis, D., Kanai, Y., & Palacı́n, M. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.10.007 · Cited by 674 · see citing works
Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family
Mastroberardino, L., Spindler, B., Pfeiffer, R., Skelly, P. J., Loffing, J., Shoemaker, C. B., & Verrey, F. (1998) · Nature · doi:10.1038/26246 · Cited by 557 · see citing works
Furukawa, H., & Gouaux, E. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg303 · Cited by 510 · see citing works
Structure of the human LAT1–4F2hc heteromeric amino acid transporter complex
Yan, R., Zhao, X., Lei, J., & Zhou, Q. (2019) · Nature · doi:10.1038/s41586-019-1011-z · Cited by 358 · see citing works
Self-citationTorrents, D., Estévez, R., Pineda, M., Fernández, E., Lloberas, J., Shi, Y., Zorzano, A., & Palacı́n, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32437 · Cited by 337 · see citing works
Non-type I cystinuria caused by mutations in SLC7A9, encoding a subunit (bo,+AT) of rBAT
Feliubadaló, L., Font, M., Purroy, J., Rousaud, F., Estivill, X., Nunes, V., Golomb, E., Centola, M. B., Aksentijevich, I. A., Kreiss, Y., et al. (1999) · Nature Genetics · doi:10.1038/12652 · Cited by 335 · see citing works
A CSF and postmortem brain study of d-serine metabolic parameters in schizophrenia
Bendikov, I., Nadri, C., Amar, S., Panizzutti, R., DEMIRANDA, J., Wolosker, H., & Agam, G. (2006) · Schizophrenia Research · doi:10.1016/j.schres.2006.10.010 · Cited by 323 · see citing works
Structure and Mechanism of a Na + -Independent Amino Acid Transporter
Shaffer, P. L., Goehring, A. S., Shankaranarayanan, A., & Gouaux, E. (2009) · Science · doi:10.1126/science.1176088 · Cited by 306 · see citing works
Lei, J., & FRANK, J. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.01.002 · Cited by 301 · see citing works
Fukasawa, Y., Segawa, H., Kim, J. Y., Chairoungdua, A., Kim, D. K., Matsuo, H., Ho, S., Endou, H., & Kanai, Y. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.13.9690 · Cited by 285 · see citing works
Structure and Mechanism of an Amino Acid Antiporter
Gao, X., Lu, F., Zhou, L., Dang, S., Sun, L., Li, X., Wang, J., & Shi, Y. (2009) · Science · doi:10.1126/science.1173654 · Cited by 229 · see citing works
Structure of a prokaryotic virtual proton pump at 3.2 Å resolution
Fang, Y., Jayaram, H., Shane, T., Kolmakova-Partensky, L., Wu, F., Williams, C., Xiong, Y., & Miller, C. (2009) · Nature · doi:10.1038/nature08201 · Cited by 220 · see citing works
Mechanism of substrate recognition and transport by an amino acid antiporter
Gao, X., Zhou, L., Jiao, X., Lu, F., Yan, C., Zeng, X. W., Wang, J., & Shi, Y. (2010) · Nature · doi:10.1038/nature08741 · Cited by 200 · see citing works
Structure and mechanism of a glutamate–GABA antiporter
Ma, D., Lu, P., Yan, C., Fan, C., Yin, P., Wang, J., & Shi, Y. (2012) · Nature · doi:10.1038/nature10917 · Cited by 200 · see citing works
The role of amino acid transporters in inherited and acquired diseases
Bröer, S., & Palacı́n, M. (2011) · Biochemical Journal · doi:10.1042/bj20101912 · Cited by 194 · see citing works
Self-citationYan, R., Xie, E., Li, Y., Li, J., Zhang, Y., Chi, X., Hu, X., Xu, L., Hou, T., Stockwell, B. R., et al. (2022) · Cell Research · doi:10.1038/s41422-022-00642-w · Cited by 184 · see citing works
Self-citationCryo-EM structure of the human L-type amino acid transporter 1 in complex with glycoprotein CD98hc
Lee, Y., Wiriyasermkul, P., Jin, C., Quan, L., Ohgaki, R., Okuda, S., Kusakizako, T., Nishizawa, T., Oda, K., Ishitani, R., et al. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0237-7 · Cited by 175 · see citing works
Kaira, K., Oriuchi, N., Imai, H., Shimizu, K., Yanagitani, N., Sunaga, N., Hisada, T., Tanaka, S., Ishizuka, T., Kanai, Y., et al. (2008) · Cancer Science · doi:10.1111/j.1349-7006.2008.00969.x · Cited by 155 · see citing works
Toyoda, M., Kaira, K., Ohshima, Y., Ishioka, N. S., Shino, M., Sakakura, K., Takayasu, Y., Takahashi, K., Tominaga, H., Oriuchi, N., et al. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.178 · Cited by 133 · see citing works
Nakauchi, J., Matsuo, H., Kim, D. K., Goto, A., Chairoungdua, A., Cha, S., Inatomi, J., Shiokawa, Y., Yamaguchi, K., Saito, I., et al. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01169-1 · Cited by 122 · see citing works
Pfeiffer, R., Spindler, B., Loffing, J., Skelly, P. J., Shoemaker, C. B., & Verrey, F. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01359-3 · Cited by 119 · see citing works
Contributions of the d-serine pathway to schizophrenia
Labrie, V., Wong, A. H. C., & Roder, J. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.01.030 · Cited by 118 · see citing works
Mechanism of substrate transport and inhibition of the human LAT1-4F2hc amino acid transporter
Yan, R., Li, Y., Müller, J., Zhang, Y., Singer, S. A., Xia, L., Zhong, X., Gertsch, J., Altmann, K., & Zhou, Q. (2021) · Cell Discovery · doi:10.1038/s41421-021-00247-4 · Cited by 103 · see citing works
Self-citationRutter, A. R., Fradley, R. L., Garrett, E., Chapman, K., Lawrence, J., Rosahl, T., & Patel, S. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05446.x · Cited by 99 · see citing works
Bröer, S. (2003) · Humana Press eBooks · doi:10.1385/1-59259-387-9:245 · Cited by 90 · see citing works
Self-citationRosell, A., Meury, M., Álvarez-Marimon, E., Costa, M., Pérez‐Cano, L., Zorzano, A., Fernández‐Recio, J., Palacı́n, M., & Fotiadis, D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1323779111 · Cited by 86 · see citing works
Kazmier, K. N., Claxton, D. P., & Mchaourab, H. S. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.12.006 · Cited by 79 · see citing works
Xie, X., Dumas, T. C., Tang, L. S., Brennan, T., Reeder, T., Thomas, W., Klein, R. D., Flores, J., O’Hara, B. F., Heller, H. C., et al. (2005) · Brain Research · doi:10.1016/j.brainres.2005.06.039 · Cited by 66 · see citing works
Amino Acid Transport Defects in Human Inherited Metabolic Disorders
Yahyaoui, R., & Frías, J. P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010119 · Cited by 66 · see citing works
Kim, D. K., Ahn, S. G., Park, J., Kanai, Y., Endou, H., & Yoon, J. H. (2004) · PubMed · Cited by 54 · see citing works
Safory, H., Neame, S., Shulman, Y., Zubedat, S., Radzishevsky, I., Rosenberg, D., Sason, H., Engelender, S., Avital, A., Hülsmann, S., et al. (2015) · The EMBO Reports · doi:10.15252/embr.201439561 · Cited by 53 · see citing works
Ehmsen, J. T., Liu, Y. U., Wang, Y., Paladugu, N., Johnson, A. E., Rothstein, J. D., du Lac, S., Mattson, M. P., & Höke, A. (2016) · Scientific Reports · doi:10.1038/srep35592 · Cited by 51 · see citing works
Cryo-EM structure of the human heteromeric amino acid transporter b 0,+ AT-rBAT
Yan, R., Li, Y., Shi, Y., Zhou, J., Lei, J., Huang, J., & Zhou, Q. (2020) · Science Advances · doi:10.1126/sciadv.aay6379 · Cited by 48 · see citing works
Self-citationStructural basis for amino acid exchange by a human heteromeric amino acid transporter
Wu, D., Grund, T. N., Welsch, S., Mills, D. J., Michel, M., Safarian, S., & Michel, H. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008111117 · Cited by 44 · see citing works
Fujita, Y., Ishima, T., & Hashimoto, K. (2016) · Scientific Reports · doi:10.1038/srep37261 · Cited by 39 · see citing works
Asc-1 regulates white versus beige adipocyte fate in a subcutaneous stromal cell population
Suwandhi, L., Altun, I., Karlina, R., Miok, V., Wiedemann, T., Fischer, D. S., Walzthoeni, T., Lindner, C., Böttcher, A., Heinzmann, S. S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21826-9 · Cited by 34 · see citing works
Oda, K., Lee, Y., Wiriyasermkul, P., Tanaka, Y., Takemoto, M., Yamashita, K., Nagamori, S., Nishizawa, T., & Nureki, O. (2020) · Protein Science · doi:10.1002/pro.3966 · Cited by 33 · see citing works
Yan, R., Zhou, J., Li, Y., Lei, J., & Zhou, Q. (2020) · Cell Discovery · doi:10.1038/s41421-020-00207-4 · Cited by 32 · see citing works
Self-citationd -serine and schizophrenia: an update
Nunes, E. A., MacKenzie, E. M., Rossolatos, D., Perez-Parada, J., Baker, G. B., & Dursun, S. M. (2012) · Expert Review of Neurotherapeutics · doi:10.1586/ern.12.65 · Cited by 32 · see citing works
Brown, J. M., Hunihan, L. W., Prack, M. M., Harden, D., Bronson, J. J., Dzierba, C. D., Gentles, R. G., Hendricson, A. W., Krause, R., Macor, J. E., et al. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12618 · Cited by 30 · see citing works
Meury, M., Costa, M., Harder, D., Stauffer, M., Jeckelmann, J.-M., Brühlmann, B., Rosell, A., İlgü, H., Kovar, K., Palacı́n, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109882 · Cited by 30 · see citing works
Sakimura, K., Nakao, K., Yoshikawa, M., Suzuki, M., & Kimura, H. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23772 · Cited by 26 · see citing works
Mikou, A., Cabayé, A., Goupil, A., Bertrand, H., Mothet, J., & Acher, F. (2020) · Scientific Reports · doi:10.1038/s41598-020-60617-y · Cited by 19 · see citing works
The neutral amino acid transporter SLC7A10 in adipose tissue, obesity and insulin resistance
Jersin, R. Å., Jonassen, L. R., & Dankel, S. N. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.974338 · Cited by 19 · see citing works
Volta Phase Plate Cryo-EM Structure of the Human Heterodimeric Amino Acid Transporter 4F2hc-LAT2
Jeckelmann, J.-M., & Fotiadis, D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040931 · Cited by 15 · see citing works
Billard, J., & Fréret, T. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14586 · Cited by 14 · see citing works
Do Amino Acid Antiporters Have Asymmetric Substrate Specificity?
Gauthier-Coles, G., Fairweather, S. J., Bröer, A., & Bröer, S. (2023) · Biomolecules · doi:10.3390/biom13020301 · Cited by 12 · see citing works
Self-citationInhibition of the Alanine-Serine-Cysteine-1 Transporter by BMS-466442
Torrecillas, I. R., Conde-Ceide, S., de Lucas, A. I., Molina, A. G., Trabanco, A. A., Lavreysen, H., Pardo, L., & Tresadern, G. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00019 · Cited by 10 · see citing works
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Pollegioni, L., Kuštrimović, N. Z., Piubelli, L., Rosini, E., Rabattoni, V., & Sacchi, S. (2025) · FEBS Journal · doi:10.1111/febs.70083 · Cited by 55 · see citing works
LAT1 transporter as a target for breast cancer diagnosis and therapy
Zhou, Z., Zhu, T., Wenlong, Z., Zou, Z., Shan, Q., Chen, Q., Wang, G., & Wang, Y. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117064 · Cited by 11 · see citing works
Dai, L., Zeng, Q., Zhang, T., Zhang, Y., Shi, Y., Li, Y., Xu, K., Huang, J., Wang, Z., Zhou, Q., et al. (2025) · Science Advances · doi:10.1126/sciadv.adq0558 · Cited by 8 · see citing works
Self-citationLu, W., Kawatani, K., Ren, Y., Nambara, T., Jia, L., Jeevaratnam, S., Lee, E., Martinez, P. R., Izhar, T., Wang, N., et al. (2026) · Alzheimer's Research & Therapy · doi:10.1186/s13195-026-01982-0 · Cited by 4 · see citing works
Self-citationFort, J., Nicolàs-Aragó, A., Maggi, L., Molledo, M. M., Kapiki, D., González-Novoa, P., Gómez-Gejo, P., Zijlstra, N., Bodoy, S., Pardon, E., et al. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae584 · Cited by 4 · see citing works
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- Authors
- Li, Y., Guo, Y., Bröer, A., Dai, L., Brӧer, S., & Yan, R.
- Affiliations
- Southern University of Science and Technology (CN)
- Australian National University (AU)
- Corresponding author
- Yan, Renhong
- Venue
- Nature Communications
- Published
- 2024-04-08
- Volume
- 15
- Issue
- 1
- Pages
- 3036-3036
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC11001984
- OpenAlex
- W4394580950
- Cited by
- 12
- References
- 61
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 2
- FWCI
- 1.93
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Westlake University
- National Natural Science Foundation of China (82202517)
- Natural Science Foundation of Guangdong Province
- Southern University of Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- 4F2hc, SLC3A2, amino acid transporters, disulfide-linked heterodimer, D-serine, L-alanine, glycine, NMDA receptor co-agonist, alternating access mechanism, substrate recognition, transporter conformational change, cryo-EM structure
- MeSH terms
- Animals, Cysteine, Glycine, Humans, Serine, Cryoelectron Microscopy, Membrane Transport Proteins, Mice
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