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• W2188103350 abstract "We have combined structural and functional approaches to investigate the role of oligomerization in the operation of the GABA transporter rGAT1. Xenopus laevis oocytes were induced to express, either separately or simultaneously, the wild-type form of rGAT1 and a mutated (Y140W) form, unable to translocate GABA and to generate transport currents, although its intram- embrane charge movement properties are only slightly affected. These characteristics, together with the insensi- tivity of Y140W to the blocking action of SKF89976A, were used to study the possible functional interaction of the two forms in an heteromeric structure. The electro- physiological data from oocytes coexpressing wild-type and Y140W rGAT1 were consistent with a completely independent activity of the two forms. Oligomerization was also studied by fl uorescence resonance energy trans- fer (FRET) in tsA201 cells expressing the transporters fused with cyan and yellow fl uorescent proteins (ECFP and EYFP). All combinations tested (WT-ECFP/WT- EYFP, Y140W-ECFP/Y140W-EYFP and WT-ECFP/ Y140W-EYFP) were able to give rise to FRET, confi rm- ing the formation of homo- as well as heterooligomers. We conclude that, although rGAT1 undergoes structural oligomerization, each monomer operates independently." @default.
• W2188103350 created "2016-06-24" @default.
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• W2188103350 date "2005-01-01" @default.
• W2188103350 modified "2023-09-27" @default.
• W2188103350 title "Research Article Functionally independent subunits in the oligomeric structure of the GABA cotransporter rGAT1" @default.
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