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J Biol Chem, Vol. 275, Issue 2, 840-846, January 14, 2000

GABA Receptor rho 1 Subunit Interacts with a Novel Splice Variant of the Glycine Transporter, GLYT-1*

Jonathan G. HanleyDagger §, Eugenia M. C. Jones§par , and Stephen J. MossDagger **

From the Dagger  Laboratory for Molecular Cell Biology and Department of Pharmacology, University College London, Gower St., London, WC1E 6BT, United Kingdom and the  Committee on Neurobiology, The University of Chicago, Chicago, Illinois

Ionotropic gamma -aminobutyric acid (GABAA and GABAC) receptors mediate fast synaptic inhibition in the central nervous system. GABAC receptors are expressed predominantly in the retina on bipolar cell axon terminals, and are thought to mediate feedback inhibition from GABAergic amacrine cells. Utilizing the yeast two-hybrid system, we previously identified MAP1B as a binding partner of the GABAC receptor rho 1 subunit. Here we describe the isolation of an additional rho 1 interacting protein: a novel C-terminal variant of the glycine transporter GLYT-1. We show that GLYT-1 exists as four alternatively spliced mRNAs which encode proteins expressing one of two possible intracellullar N- and C-terminal domains. Variants containing the novel C terminus efficiently transport glycine when expressed in COS cells, but with unusual kinetics. We have confirmed the interaction between the novel C terminus and rho 1 subunit and demonstrated binding in heterologous cells. This interaction may be crucial for the integration of GABAergic and glycinergic neurotransmission in the retina.


* This work was supported by the Medical Research Council, the Wellcome Trust, and the Royal Society.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Contributed equally to the results of this work.

par Present address: Dept. of Physiology, University of Wisconsin, Madison, WI.

** To whom correspondence should be addressed: MRC-LMCB, University College London, Gower St., London, WC1E 6BT United Kingdom. Fax.: 44-171-380-7805; E-mail: steve.moss@ucl.ac.uk.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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