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Molecular Determinants for Substrate Interactions with the Glycine Transporter GlyT2
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    Research Article

    Molecular Determinants for Substrate Interactions with the Glycine Transporter GlyT2
    Click to copy article linkArticle link copied!

    • Jane E. Carland
      Jane E. Carland
      Discipline of Pharmacology, School of Medical Sciences, Molecular Biosciences Building, University of Sydney, Sydney, NSW 2006, Australia
    • Michael Thomas
      Michael Thomas
      Research School of Chemistry, The Australian National University, Canberra, ACT 0200, Australia
    • Shannon N. Mostyn
      Shannon N. Mostyn
      Discipline of Pharmacology, School of Medical Sciences, Molecular Biosciences Building, University of Sydney, Sydney, NSW 2006, Australia
    • Nandhitha Subramanian
      Nandhitha Subramanian
      Research School of Chemistry, The Australian National University, Canberra, ACT 0200, Australia
    • Megan L. O’Mara
      Megan L. O’Mara
      Research School of Chemistry, The Australian National University, Canberra, ACT 0200, Australia
    • Renae M. Ryan
      Renae M. Ryan
      Discipline of Pharmacology, School of Medical Sciences, Molecular Biosciences Building, University of Sydney, Sydney, NSW 2006, Australia
    • Robert J. Vandenberg*
      Robert J. Vandenberg
      Discipline of Pharmacology, School of Medical Sciences, Molecular Biosciences Building, University of Sydney, Sydney, NSW 2006, Australia
      *Robert Vandenberg. Tel: 61-2-9351-6734. E-mail: [email protected]
    Other Access OptionsSupporting Information (1)

    ACS Chemical Neuroscience

    Cite this: ACS Chem. Neurosci. 2018, 9, 3, 603–614
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    https://doi.org/10.1021/acschemneuro.7b00407
    Published November 9, 2017
    Copyright © 2017 American Chemical Society

    Abstract

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    Transporters in the SLC6 family play key roles in regulating neurotransmission and are the targets for a wide range of therapeutics. Important insights into the transport mechanisms and the specificity of drug interactions of SLC6 transporters have been obtained from the crystal structures of a bacterial homologue of the family, LeuTAa, and more recently the Drosophila dopamine transporter and the human serotonin transporter. However, there is disputed evidence that the bacterial leucine transporter, LeuTAa, contains two substrate binding sites that work cooperatively in the mechanism of transport, with the binding of a second substrate being required for the release of the substrate from the primary site. An alternate proposal is that there may be low affinity binding sites that serve to direct the flow of substrates to the primary site. We have used a combination of molecular dynamics simulations of substrate interactions with a homology model of GlyT2, together with radiolabeled amino acid uptake assays and electrophysiological analysis of wild-type and mutant transporters, to provide evidence that substrate selectivity of GlyT2 is determined entirely by the primary substrate binding site and, furthermore, if a secondary site exists then it is a low affinity nonselective amino acid binding site.

    Copyright © 2017 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acschemneuro.7b00407.

    • Discussion of the investigation into whether the GlyT2 model forms similar structures to both the outward occluded and outward open structures of LeuTAa (PDF)

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    Cited By

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    This article is cited by 23 publications.

    1. Cristina Benito-Muñoz, Almudena Perona, Raquel Felipe, Gonzalo Pérez-Siles, Enrique Núñez, Carmen Aragón, Beatriz López-Corcuera. Structural Determinants of the Neuronal Glycine Transporter 2 for the Selective Inhibitors ALX1393 and ORG25543. ACS Chemical Neuroscience 2021, 12 (11) , 1860-1872. https://doi.org/10.1021/acschemneuro.0c00602
    2. Shannon N. Mostyn, Subhodeep Sarker, Parthasarathy Muthuraman, Arun Raja, Susan Shimmon, Tristan Rawling, Christopher L. Cioffi, Robert J. Vandenberg. Photoswitchable ORG25543 Congener Enables Optical Control of Glycine Transporter 2. ACS Chemical Neuroscience 2020, 11 (9) , 1250-1258. https://doi.org/10.1021/acschemneuro.9b00655
    3. Filip Fratev, Manuel Miranda-Arango, Ashley Bryan Lopez, Elvia Padilla, Suman Sirimulla. Discovery of GlyT2 Inhibitors Using Structure-Based Pharmacophore Screening and Selectivity Studies by FEP+ Calculations. ACS Medicinal Chemistry Letters 2019, 10 (6) , 904-910. https://doi.org/10.1021/acsmedchemlett.9b00003
    4. Alexandra Schumann-Gillett, Megan L. O’Mara. Lipid-Based Inhibitors Act Directly on GlyT2. ACS Chemical Neuroscience 2019, 10 (3) , 1668-1678. https://doi.org/10.1021/acschemneuro.8b00586
    5. Shannon N. Mostyn, Tristan Rawling, Sarasa Mohammadi, Susan Shimmon, Zachary J. Frangos, Subhodeep Sarker, Arsalan Yousuf, Irina Vetter, Renae M. Ryan, Macdonald J. Christie, Robert J. Vandenberg. Development of an N-Acyl Amino Acid That Selectively Inhibits the Glycine Transporter 2 To Produce Analgesia in a Rat Model of Chronic Pain. Journal of Medicinal Chemistry 2019, 62 (5) , 2466-2484. https://doi.org/10.1021/acs.jmedchem.8b01775
    6. Yiqing Wei, Renjie Li, Yufei Meng, Tuo Hu, Jun Zhao, Yiwei Gao, Qinru Bai, Na Li, Yan Zhao. Transport mechanism and pharmacology of the human GlyT1. Cell 2024, 187 (7) , 1719-1732.e14. https://doi.org/10.1016/j.cell.2024.02.026
    7. Ryan Cantwell Chater, Ada S. Quinn, Katie Wilson, Zachary J. Frangos, Patrick Sutton, Srinivasan Jayakumar, Christopher L. Cioffi, Megan L. O'Mara, Robert J. Vandenberg. The efficacy of the analgesic GlyT2 inhibitor, ORG25543 , is determined by two connected allosteric sites. Journal of Neurochemistry 2023, 12 https://doi.org/10.1111/jnc.16028
    8. Zachary J Frangos, Katie A Wilson, Heather M Aitken, Ryan Cantwell Chater, Robert J Vandenberg, Megan L O’Mara. Membrane cholesterol regulates inhibition and substrate transport by the glycine transporter, GlyT2. Life Science Alliance 2023, 6 (4) , e202201708. https://doi.org/10.26508/lsa.202201708
    9. Bastien Le Guellec, France Rousseau, Marion Bied, Stéphane Supplisson. Flux coupling, not specificity, shapes the transport and phylogeny of SLC6 glycine transporters. Proceedings of the National Academy of Sciences 2022, 119 (41) https://doi.org/10.1073/pnas.2205874119
    10. Catriona M. H. Anderson, Noel Edwards, Andrew K. Watson, Mike Althaus, David T. Thwaites. Reshaping the Binding Pocket of the Neurotransmitter:Solute Symporter (NSS) Family Transporter SLC6A14 (ATB0,+) Selectively Reduces Access for Cationic Amino Acids and Derivatives. Biomolecules 2022, 12 (10) , 1404. https://doi.org/10.3390/biom12101404
    11. Deepthi Joseph, Smruti Ranjan Nayak, Aravind Penmatsa. Structural insights into GABA transport inhibition using an engineered neurotransmitter transporter. The EMBO Journal 2022, 41 (15) https://doi.org/10.15252/embj.2022110735
    12. Kamil Łątka, Marek Bajda. Analysis of Binding Determinants for Different Classes of Competitive and Noncompetitive Inhibitors of Glycine Transporters. International Journal of Molecular Sciences 2022, 23 (14) , 8050. https://doi.org/10.3390/ijms23148050
    13. Zachary J. Frangos, Ryan P. Cantwell Chater, Robert J. Vandenberg. Glycine Transporter 2: Mechanism and Allosteric Modulation. Frontiers in Molecular Biosciences 2021, 8 https://doi.org/10.3389/fmolb.2021.734427
    14. Azadeh Shahsavar, Peter Stohler, Gleb Bourenkov, Iwan Zimmermann, Martin Siegrist, Wolfgang Guba, Emmanuel Pinard, Steffen Sinning, Markus A. Seeger, Thomas R. Schneider, Roger J. P. Dawson, Poul Nissen. Structural insights into the inhibition of glycine reuptake. Nature 2021, 591 (7851) , 677-681. https://doi.org/10.1038/s41586-021-03274-z
    15. Katie A. Wilson, Shannon N. Mostyn, Zachary J. Frangos, Susan Shimmon, Tristan Rawling, Robert J. Vandenberg, Megan L. O’Mara. The allosteric inhibition of glycine transporter 2 by bioactive lipid analgesics is controlled by penetration into a deep lipid cavity. Journal of Biological Chemistry 2021, 296 , 100282. https://doi.org/10.1016/j.jbc.2021.100282
    16. Claire Colas. Toward a Systematic Structural and Functional Annotation of Solute Carriers Transporters—Example of the SLC6 and SLC7 Families. Frontiers in Pharmacology 2020, 11 https://doi.org/10.3389/fphar.2020.01229
    17. Martina Baliova, Frantisek Jursky. Phosphorylation of Serine 157 Protects the Rat Glycine Transporter GlyT2 from Calpain Cleavage. Journal of Molecular Neuroscience 2020, 70 (8) , 1216-1224. https://doi.org/10.1007/s12031-020-01529-4
    18. Stephen J. Fairweather, Nishank Shah, Stefan Brӧer. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology. 2020, 13-127. https://doi.org/10.1007/5584_2020_584
    19. Shannon N Mostyn, Katie A Wilson, Alexandra Schumann-Gillett, Zachary J Frangos, Susan Shimmon, Tristan Rawling, Renae M Ryan, Megan L O'Mara, Robert J Vandenberg. Identification of an allosteric binding site on the human glycine transporter, GlyT2, for bioactive lipid analgesics. eLife 2019, 8 https://doi.org/10.7554/eLife.47150
    20. Michael V. LeVine, Daniel S. Terry, George Khelashvili, Zarek S. Siegel, Matthias Quick, Jonathan A. Javitch, Scott C. Blanchard, Harel Weinstein. The allosteric mechanism of substrate-specific transport in SLC6 is mediated by a volumetric sensor. Proceedings of the National Academy of Sciences 2019, 116 (32) , 15947-15956. https://doi.org/10.1073/pnas.1903020116
    21. Alexandra Schumann-Gillett, Mitchell T. Blyth, Megan L. O’Mara. Is protein structure enough? A review of the role of lipids in SLC6 transporter function. Neuroscience Letters 2019, 700 , 64-69. https://doi.org/10.1016/j.neulet.2018.05.020
    22. Beatriz López-Corcuera, Esther Arribas-González, Carmen Aragón. Hyperekplexia-associated mutations in the neuronal glycine transporter 2. Neurochemistry International 2019, 123 , 95-100. https://doi.org/10.1016/j.neuint.2018.05.014
    23. Cristina Benito-Muñoz, Almudena Perona, David Abia, Helena G. dos Santos, Enrique Núñez, Carmen Aragón, Beatriz López-Corcuera. Modification of a Putative Third Sodium Site in the Glycine Transporter GlyT2 Influences the Chloride Dependence of Substrate Transport. Frontiers in Molecular Neuroscience 2018, 11 https://doi.org/10.3389/fnmol.2018.00347

    ACS Chemical Neuroscience

    Cite this: ACS Chem. Neurosci. 2018, 9, 3, 603–614
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acschemneuro.7b00407
    Published November 9, 2017
    Copyright © 2017 American Chemical Society

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