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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1997-5-2
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pubmed:abstractText |
We have previously shown that direct binding of the betagamma subunit of G protein (G betagamma) to both the N-terminal domain and the C-terminal domain of a cloned G protein-gated inward-rectifying K+ channel subunit, GIRK1, is important for channel activation. We have now further localized the G betagamma binding region in the N-terminal domain of GIRK1 to amino acids 34-86 and the G betagamma binding region in the C-terminal domain of GIRK1 to two separate fragments of amino acids 318-374 and amino acids 390-462. Of the four cloned mammalian GIRK subunits, GIRK1-4, GIRK1 and 4 form heteromeric K+ channels in the heart and similar channels in the brain include heteromultimers of GIRK1 and 2, and possibly other GIRK homomultimers and heteromultimers. We found that the N-terminal and the C-terminal domains of all four GIRKs bound G betagamma. The G betagamma binding activities for the C-terminal domains of GIRK2-4 were lower than that for the C-terminal domain of GIRK1. The higher G betagamma binding activity for the C-terminal domain of GIRK1 is due to amino acids 390-462 which are unique to GIRK1. We also found that the N-terminal and C-terminal domains of GIRKs interacted with each other, and the N-terminal domain of either GIRK1 or GIRK4 together with the C-terminal domain of GIRK1 exhibited much enhanced binding of G betagamma. These results are consistent with the idea that the N- and C-terminal domains of the cardiac G protein-gated K+ channel subunits may interact with each other to form higher affinity binding site(s) for G betagamma.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/G Protein-Coupled...,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/KCNJ3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
405
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
291-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9108307-Amino Acid Sequence,
pubmed-meshheading:9108307-Animals,
pubmed-meshheading:9108307-Binding Sites,
pubmed-meshheading:9108307-Cattle,
pubmed-meshheading:9108307-G Protein-Coupled Inwardly-Rectifying Potassium Channels,
pubmed-meshheading:9108307-GTP-Binding Proteins,
pubmed-meshheading:9108307-Ion Channel Gating,
pubmed-meshheading:9108307-Macromolecular Substances,
pubmed-meshheading:9108307-Molecular Sequence Data,
pubmed-meshheading:9108307-Potassium Channels,
pubmed-meshheading:9108307-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:9108307-Protein Binding,
pubmed-meshheading:9108307-Recombinant Fusion Proteins,
pubmed-meshheading:9108307-Sequence Alignment,
pubmed-meshheading:9108307-Sequence Homology, Amino Acid
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pubmed:year |
1997
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pubmed:articleTitle |
Binding of the G protein betagamma subunit to multiple regions of G protein-gated inward-rectifying K+ channels.
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pubmed:affiliation |
Department of Physiology, the University of California at San Francisco, 94143-0724, USA. chuan1@mednet.swmed.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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