Affiliation:
1. Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR 97239
Abstract
Significance
Glutamate transporters harness ionic gradients present across the membrane for the rapid removal of glutamate from the synaptic space. Normal function of glutamate transporters is required for efficient synaptic transmission and preventing excitotoxicity. Central to the transport mechanism is the coupled binding of Na
+
and the substrate. While structural studies have identified the Na
+
and the substrate binding sites, the mechanism by which Na
+
and substrate binding is coupled is not known. In this study, we developed assays to monitor Na
+
binding and to track key conformational changes in Glt
Ph
, an archaeal homolog of glutamate transporters. We use these assays along with previously developed assays to describe the specific roles of the Na
+
sites in the coupling mechanism.
Funder
HHS | NIH | National Institute of General Medical Sciences
HHS | NIH | National Institute of Neurological Disorders and Stroke
American Heart Association
Publisher
Proceedings of the National Academy of Sciences
Cited by
1 articles.
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