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XB-ART-5378
Neuron 2003 Apr 24;382:225-35. doi: 10.1016/s0896-6273(03)00193-4.
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Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy.

Riven I , Kalmanzon E , Segev L , Reuveny E .


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G protein-coupled potassium channels (GIRK/Kir3.x) are key determinants that translate inhibitory chemical neurotransmission into changes in cellular excitability. To understand the mechanism of channel activation by G proteins, it is necessary to define the structural rearrangements in the channel that result from interaction with Gbetagamma subunits. In this study we used a combination of fluorescence spectroscopy and through-the-objective total internal reflection microscopy to monitor the conformational rearrangements associated with the activation of GIRK channels in single intact cells. We detect activation-induced changes in FRET consistent with a rotation and expansion of the termini along the central axis of the channel. We propose that this rotation and expansion of the termini drives the channel to open by bending and possibly rotating the second transmembrane segment.

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Species referenced: Xenopus laevis
Genes referenced: kcnj3

References :
Evans, New turf for CFP/YFP FRET imaging of membrane signaling molecules. 2003, Pubmed