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Publication Detail
GABA_{C} Receptor Sensitivity Is Modulated by Interaction with MAP1B
GABA_{C} receptors contain ρ subunits and mediate feedback inhibition from retinal amacrine cells to bipolar cells. We previously identified the cytoskeletal protein MAP1B as a ρ1 subunit anchoring protein. Here, we analyze the structural basis and functional significance of the MAP1B-ρ1 interaction. Twelve amino acids at the C terminus of the large intracellular loop of ρ1 (and also ρ2) are sufficient for interaction with MAP1B. Disruption of the MAP1B-ρ interaction in bipolar cells in retinal slices decreased the EC₅₀ of their GABA_{C} receptors, doubling the receptors' current at low GABA concentrations without affecting their maximum current at high concentrations. Thus, anchoring to the cytoskeleton lowers the sensitivity of GABA_{C} receptors and provides a likely site for functional modulation of GABA_{C}receptor-mediated inhibition.
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