Source:http://linkedlifedata.com/resource/pubmed/id/16950155
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2006-9-4
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pubmed:abstractText |
G protein-coupled signaling is one of the major mechanisms for controlling cellular excitability. One of the main targets for this control at postsynaptic membranes is the G protein-coupled potassium channels (GIRK/Kir3), which generate slow inhibitory postsynaptic potentials following the activation of Pertussis toxin-sensitive G protein-coupled receptors. Using total internal reflection fluorescence (TIRF) microscopy combined with fluorescence resonance energy transfer (FRET), in intact cells, we provide evidence for the existence of a trimeric G protein-channel complex at rest. We show that activation of the channel via the receptor induces a local conformational switch of the G protein to induce channel opening. The presence of such a complex thus provides the means for a precise temporal and highly selective activation of the channel, which is required for fine tuning of neuronal excitability.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0896-6273
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
51
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
561-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16950155-Cell Line,
pubmed-meshheading:16950155-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:16950155-G Protein-Coupled Inwardly-Rectifying Potassium Channels,
pubmed-meshheading:16950155-GTP-Binding Proteins,
pubmed-meshheading:16950155-Humans,
pubmed-meshheading:16950155-Membrane Potentials,
pubmed-meshheading:16950155-Microscopy, Fluorescence,
pubmed-meshheading:16950155-Neurons,
pubmed-meshheading:16950155-Patch-Clamp Techniques,
pubmed-meshheading:16950155-Protein Structure, Quaternary,
pubmed-meshheading:16950155-Signal Transduction
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pubmed:year |
2006
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pubmed:articleTitle |
GIRK channel activation involves a local rearrangement of a preformed G protein channel complex.
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pubmed:affiliation |
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel 76100.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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