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Role of Heteromer Formation in GABA B Receptor Function
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.
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Metadata
- Authors
- Kuner, R., Köhr, G., Grünewald, S., Eisenhardt, G., Bach, A., & Kornau, H.-C.
- Venue
- Science
- Published
- 1999-01
- Volume
- 283
- Issue
- 5398
- Pages
- 74-77
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2084240593
- Cited by
- 562
- References
- 0
- FWCI
- 22.94
- Type
- journal article
- Language
- en
- Open access
- closed
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- Kuner, R., Köhr, G., Grünewald, S., Eisenhardt, G., Bach, A., & Kornau, H.-C. (1999). Role of Heteromer Formation in GABA B Receptor Function. Science. https://doi.org/10.1126/science.283.5398.74
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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