期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 14, 期 5, 页码 365-371出版社
NATURE PORTFOLIO
DOI: 10.1038/nsmb1230
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Glutamate transporters (EAATs) are pivotal in mammalian synaptic transmission, tightly regulating synaptic levels of this excitatory neurotransmitter. In addition to coupled glutamate transport, the EAATs also show an uncoupled Cl- conductance, whose physiological importance has recently been demonstrated. Little is yet known about the molecular mechanism of chloride permeation. Here we show that Glt(Ph), a bacterial EAAT homolog whose structure has been determined, displays an uncoupled Cl- conductance that can determine the rate of substrate uptake. A mutation analogous to one known to specifically affect Cl movement in EAAT1 has similar effects on GltPh, suggesting that this protein is an excellent structural model for understanding Cl- permeation through the EAATs. We also observed an uncoupled Cl- conductance in another bacterial EAAT homolog but not in a homolog of the Na+/Cl--coupled neurotransmitter transporters.
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