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The Journal of Neuroscience, December 1, 2000, 20(23):8643-8650
GABAC Receptor Sensitivity Is Modulated by
Interaction with MAP1B
Daniela
Billups1, 2,
Jonathan G.
Hanley1,
Mariam
Orme1,
David
Attwell2, and
Stephen J.
Moss1
1 Laboratory for Molecular Cell Biology and Department
of Pharmacology, and 2 Department of Physiology, University
College London, London, WC1E 6BT, United Kingdom
GABAC receptors contain  subunits and mediate
feedback inhibition from retinal amacrine cells to bipolar cells. We
previously identified the cytoskeletal protein MAP1B as a 1 subunit
anchoring protein. Here, we analyze the structural basis and functional significance of the MAP1B-1 interaction. Twelve amino acids at the C
terminus of the large intracellular loop of 1 (and also 2) are
sufficient for interaction with MAP1B. Disruption of the MAP1B-
interaction in bipolar cells in retinal slices decreased the
EC50 of their GABAC 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 GABAC receptors and
provides a likely site for functional modulation of GABAC
receptor-mediated inhibition.
Key words:
GABA; subunit; MAP1B; EC50; retina; bipolar; uptake
Copyright © 2000 Society for Neuroscience 0270-6474/00/20238643-08$05.00/0
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