Journal article
Evidence that direct binding of G βγ to the GIRK1 G protein-gated inwardly rectifying K + channel is important for channel activation
Neuron (Cambridge, Mass.), Vol.15(5), pp.1133-1143
1995
DOI: 10.1016/0896-6273(95)90101-9
Abstract
Activation of G protein-gated K
+ channels by G protein-coupled receptors contributes to parasympathetic regulation of heart rate in the atrium and inhibitory postsynaptic potentials in the peripheral and central nervous system. Having found that G
βγ activates the cloned GIRK1 channel, we now report evidence for direct binding of G
βγ to both the N-terminal hydrophilic domain and amino acids 273–462 of the C-terminal domain of GIRK1. These direct interactions are physiologically important because synthetic peptides derived from either domain reduce the G
βγ binding as well as the G
βγ activation of the channel. Moreover, the N-terminal domain may also bind trimeric G
αβγ, raising the possibility that physical association of G protein-coupled receptors, G proteins, and K
+ channels partially accounts for their compartmentalization and hence rapid and specific channel activation by receptors.
Details
- Title: Subtitle
- Evidence that direct binding of G βγ to the GIRK1 G protein-gated inwardly rectifying K + channel is important for channel activation
- Creators
- Chou-Long Huang - University of California, San FranciscoPaul A. Slesinger - University of California, San FranciscoPatrick J. Casey - Duke UniversityYuh Nung Jan - University of California, San FranciscoLily Y. Jan - University of California, San Francisco
- Resource Type
- Journal article
- Publication Details
- Neuron (Cambridge, Mass.), Vol.15(5), pp.1133-1143
- DOI
- 10.1016/0896-6273(95)90101-9
- ISSN
- 0896-6273
- eISSN
- 1097-4199
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 1995
- Academic Unit
- Nephrology; Internal Medicine
- Record Identifier
- 9984360044802771
Metrics
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