GABAC受体敏感性通过与微管相关蛋白1B相互作用来调节。
GABAC receptor sensitivity is modulated by interaction with MAP1B.
作者信息
Billups D, Hanley J G, Orme M, Attwell D, Moss S J
机构信息
Laboratory for Molecular Cell Biology, Department of Pharmacology, University College London, London, WC1E 6BT, United Kingdom.
出版信息
J Neurosci. 2000 Dec 1;20(23):8643-50. doi: 10.1523/JNEUROSCI.20-23-08643.2000.
Abstract
GABA(C) receptors contain rho subunits and mediate feedback inhibition from retinal amacrine cells to bipolar cells. We previously identified the cytoskeletal protein MAP1B as a rho1 subunit anchoring protein. Here, we analyze the structural basis and functional significance of the MAP1B-rho1 interaction. Twelve amino acids at the C terminus of the large intracellular loop of rho1 (and also rho2) are sufficient for interaction with MAP1B. Disruption of the MAP1B-rho 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.
摘要
GABA(C)受体含有rho亚基，并介导从视网膜无长突细胞到双极细胞的反馈抑制。我们之前鉴定出细胞骨架蛋白MAP1B是一种rho1亚基锚定蛋白。在此，我们分析MAP1B-rho1相互作用的结构基础和功能意义。rho1（以及rho2）大的细胞内环C末端的12个氨基酸足以与MAP1B相互作用。视网膜切片中双极细胞内MAP1B-rho相互作用的破坏降低了其GABA(C)受体的半数有效浓度（EC(50)），在低GABA浓度下使受体电流加倍，而不影响高浓度下的最大电流。因此，与细胞骨架的锚定降低了GABA(C)受体的敏感性，并为GABA(C)受体介导的抑制的功能调节提供了一个可能的位点。
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