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- W2797489511 abstract "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 EC 50 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." @default.
- W2797489511 created "2018-04-24" @default.
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- W2797489511 date "2000-12-01" @default.
- W2797489511 modified "2023-10-18" @default.
- W2797489511 title "GABA<sub>C</sub>Receptor Sensitivity Is Modulated by Interaction with MAP1B" @default.
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- W2797489511 doi "https://doi.org/10.1523/jneurosci.20-23-08643.2000" @default.
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