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• W3152466469 abstract "Secondary active transporters reside in cell membranes transporting polar solutes like amino acids against steep concentration gradients, using electrochemical gradients of ions as energy sources. Commonly, ensemble-based measurements of radiolabeled substrate uptakes or transport currents inform on kinetic parameters of transporters. Here we describe a fluorescence-based functional assay for glutamate and aspartate transporters that provides single-transporter, single-transport cycle resolution using an archaeal elevator-type sodium and aspartate symporter GltPh as a model system. We prepare proteo-liposomes containing reconstituted purified GltPh transporters and an encapsulated periplasmic glutamate/aspartate-binding protein, PEB1a, labeled with donor and acceptor fluorophores. We then surface-immobilize the proteo-liposomes and measure transport-dependent Fluorescence Resonance Energy Transfer (FRET) efficiency changes over time using single-molecule Total Internal Reflection Fluorescence (TIRF) microscopy. The assay provides a 10-100 fold increase in temporal resolution compared to radioligand uptake assays. It also allows kinetic characterization of different transport cycle steps and discerns kinetic heterogeneities within the transporter population." @default.
• W3152466469 created "2021-04-13" @default.
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• W3152466469 date "2021-01-01" @default.
• W3152466469 modified "2023-10-16" @default.
• W3152466469 title "FRET-based Microscopy Assay to Measure Activity of Membrane Amino Acid Transporters with Single-transporter Resolution" @default.
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• W3152466469 doi "https://doi.org/10.21769/bioprotoc.3970" @default.
• W3152466469 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8054209" @default.
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• W3152466469 hasPublicationYear "2021" @default.
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