Abstract
An established membrane potential is fundamental to the survival of a cell. The majority of cellular and physiological processes foremost require orchestration of various ion channel activities and interactions in a spatially and temporally interdependent fashion. Previously we found that Vpu, a single transmembrane protein encoded by HIV-1, could interact with the assembly of endogenous K2P channels that set resting potentials. This Vpu function reflects its viroporin structure, conferring the propensity to oligomerize into homomeric channels or promiscuously with homologous endogenous channel subunits. By interfering with normal assembly of background K+ channels, Vpu suppresses the stabilizing K+ conductance and dissipates the transmembrane voltage constraint on viral particle discharge. In this report, we measured membrane potential changes with respect to TASK-Vpu interaction in single cells by implementing a FRET pair with potential-tracking imaging. Our combined measurements from FLIM/FRET and confocal microscopy showed a structural-functional coupling between the two physical parameters (protein-protein interaction; membrane potential), and confirmed the previous experimental results obtained by independent means.
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