Ion transport and regulation in a synaptic vesicle glutamate transporter
Autor: | Alisa Bowen, Alexander G. Myasnikov, Phuong Nguyen, Roger Chang, David Bulkley, Robert H. Edwards, Janet Finer-Moore, Fei Li, Zanlin Yu, Robert M. Stroud, Yifan Cheng, Jacob Eriksen |
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Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
Neurotransmitter transporter Glutamic Acid Neurotransmission Synaptic vesicle Exocytosis Article Membrane Potentials 03 medical and health sciences 0302 clinical medicine Allosteric Regulation Chlorides Protein Domains Chloride Channels Animals Amino Acid Sequence Membrane potential Multidisciplinary Binding Sites Ion Transport Chemistry Cryoelectron Microscopy Glutamate receptor Glutamate binding Hydrogen-Ion Concentration Synaptic vesicle cycle Rats 030104 developmental biology Biophysics Vesicular Glutamate Transport Protein 2 Synaptic Vesicles 030217 neurology & neurosurgery |
Zdroj: | Science |
ISSN: | 1095-9203 |
Popis: | Transport dependent on context Transporter proteins move substrates across a membrane, often coupling this activity to cellular ion concentration gradients. For neurotransmitter transporters, which reside in synaptic vesicles that fuse with the plasma membrane after an action potential, transport activity needs to be regulated so that they do not pump out neurotransmitters after vesicle fusion. Using cryo–electron microscopy, Li et al. determined the structure of a vesicular glutamate transporter from rat that unveils some of the distinctive features that enable it to function properly in two distinct cellular environments. An allosteric pH sensor, proposed to be a glutamate residue, gates binding of the substrate glutamate and simultaneously permits binding and counterflow of chloride ions. This molecular traffic light allows for a single ion channel to behave appropriately in different contexts. Science , this issue p. 893 |
Databáze: | OpenAIRE |
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