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  Role of heteromer formation in GABAB receptor function

Kuner, R., Köhr, G., Grünewald, S., Eisenhardt, G., Bach, A. W. J., & Kornau, H. C. (1999). Role of heteromer formation in GABAB receptor function. Science, 283(5398), 74-77. doi:10.1126/science.283.5398.74.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A38B-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-A1EA-8
Genre: Journal Article

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Science_283_1999_74.pdf (Any fulltext), 180KB
 
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Kuner, Rohini, Author
Köhr, Georg1, 2, 3, Author              
Grünewald, Sabine1, Author              
Eisenhardt, G., Author
Bach, Alfred W. J., Author
Kornau, Hans Christian1, Author              
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Directly responsible to the Managing Director, Max Planck Institute for Medical Research, Max Planck Society, ou_persistent22              
3Georg Köhr Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497714              

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 Abstract: Recently, GBR1, a seven-transmembrane domain protein with high affinity for gamma-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 GABAB 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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Language(s): eng - English
 Dates: 1998-11-181998-12-071999-01-01
 Publication Status: Published in print
 Pages: 4
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 Rev. Method: Peer
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Title: Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 283 (5398) Sequence Number: - Start / End Page: 74 - 77 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1