Transporters in the nervous system articles within Nature

Featured

  • Article |

    Monoamines and neurotoxicants share a binding pocket in VMAT1 featuring polar sites for specificity and a wrist-and-fist shape for versatility, and monoamine enrichment in storage vesicles arises from dominant import via favoured lumenal-open transition of VMAT1 and protonation-precluded binding during its cytoplasmic-open transition.

    • Jin Ye
    • , Huaping Chen
    •  & Weikai Li

  • Article |

    Serial synchrotron crystallography reveals the structure of the human glycine transporter GlyT1, showing how a state-specific inhibitor exerts its effects, and potentially informing the design of new GlyT1 inhibitors to treat a range of disorders of the central nervous system.

    • Azadeh Shahsavar
    • , Peter Stohler
    •  & Poul Nissen

  • Article |

    The lysosomal polyamine transporter ATP13A2 controls the cellular polyamine content, and impaired lysosomal polyamine export represents a lysosome-dependent cell death pathway that may be implicated in ATP13A2-associated neurodegeneration.

    • Sarah van Veen
    • , Shaun Martin
    •  & Peter Vangheluwe

  • Article |

    X-ray crystal structures of the human serotonin transporter (SERT) bound to the antidepressants (S)-citalopram or paroxetine show that the antidepressants lock the protein in an outward-open conformation, and directly block serotonin from entering its binding site; the structures define the mechanism of antidepressant action in SERT and pave the way for future drug design.

    • Jonathan A. Coleman
    • , Evan M. Green
    •  & Eric Gouaux

  • Letter |

    The X-ray crystal structure of the glutamate–GABA antiporter GadC is determined, revealing an inward-open conformation and providing insights into mechanism of amino acid antiport that is needed for acid resistance in bacteria.

    • Dan Ma
    • , Peilong Lu
    •  & Yigong Shi

  • Letter |

    The initial crystal structure of LeuT, together with subsequent functional and structural studies, provided direct evidence for a single, high-affinity substrate-binding site. Recent binding, flux and molecular simulation studies, however, have been interpreted in terms of a model where there are two high-affinity binding sites: the second (S2) site is believed to be located within the extracellular vestibule. Here, direct measurement is performed of substrate binding to wild-type LeuT and to S2 site mutants using isothermal titration calorimetry, equilibrium dialysis and scintillation proximity assays. The conclusion is made that LeuT harbours a single, centrally located, high-affinity substrate-binding site.

    • Chayne L. Piscitelli
    • , Harini Krishnamurthy
    •  & Eric Gouaux

  • Article |

    Neurotransmitter:Na+ symporters (NSS) remove neurotransmitters from the synapse in a reuptake process that is driven by the Na+ gradient. Here, single-molecule fluorescence imaging assays have been combined with molecular dynamics simulations to probe the conformational changes that are associated with substrate binding and transport by a prokaryotic NSS homologue, LeuT. The findings are interpreted in the context of an allosteric mechanism that couples ion and substrate binding to transport.

    • Yongfang Zhao
    • , Daniel Terry
    •  & Jonathan A. Javitch

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