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pubmed-article:1970294pubmed:abstractTextActive accumulation of neurotransmitters by synaptic vesicles is an essential component of the synaptic transmission cycle. Isolated vesicles show energy-dependent uptake of several transmitters by processes which are apparently mediated by a proton electrochemical potential across the vesicle membrane. Although this energy gradient is probably generated by a proton ATPase, the functional separation of ATP cleavage and transmitter uptake activity has only been shown clearly for monoamine transport. We report here that the light-driven proton pump, bacteriorhodopsin, can replace the endogenous proton ATPase in proteoliposomes reconstituted from vesicular detergent extracts. The system shows light-dependent uptake of glutamate with properties very similar to those observed in intact vesicles, e.g. chloride dependence or stimulation by NH4+. Our experiments show that the proton pump and the glutamate transporter are separate entities and provide a powerful tool for further characterization of the glutamate carrier.lld:pubmed
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pubmed-article:1970294pubmed:pagination1465-9lld:pubmed
pubmed-article:1970294pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:1970294pubmed:articleTitleBacteriorhodopsin drives the glutamate transporter of synaptic vesicles after co-reconstitution.lld:pubmed
pubmed-article:1970294pubmed:affiliationDepartment of Neurochemistry, Max-Planck-Institute for Psychiatry, Martinsried, FRG.lld:pubmed
pubmed-article:1970294pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1970294pubmed:publicationTypeIn Vitrolld:pubmed
pubmed-article:1970294pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed