Role of Heteromer Formation in GABA B Receptor Function
- 1 January 1999
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 283 (5398), 74-77
- https://doi.org/10.1126/science.283.5398.74
Abstract
Recently, GBR1, a seven-transmembrane domain protein with high affinity for γ-aminobutyric acid (GABA) B receptor antagonists, was identified. Here, a GBR1-related protein, GBR2, was shown to be coexpressed with GBR1 in many brain regions and to interact with it through a short domain in the carboxyl-terminal cytoplasmic tail. Heterologously expressed GBR2 mediated inhibition of adenylyl cyclase; however, inwardly rectifying potassium channels were activated by GABA B receptor agonists only upon coexpression with GBR1 and GBR2. Thus, the interaction of these receptors appears to be crucial for important physiological effects of GABA and provides a mechanism in receptor signaling pathways that involve a heterotrimeric GTP-binding protein.Keywords
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