Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1996-11-25
|
pubmed:abstractText |
The cardiac inward rectifying K+ channel, CIR, and the strongly inward rectifying K+ channel, IRK1, exhibited clearly different electrophysiological properties. CIR formed a heteromultimer with the G-protein coupled inward rectifying K+ channel, GIRK1, whereas IRK1 did not, and CTR homo- and heteromultimeric channels were activated by G-protein beta 1 gamma 2 subunits (G beta 1 gamma 2), whereas IRK1 channels were not. To identify the domains of CIR involved in the heteromultimer formation with GIRK1 and in the G beta 1 gamma 2 gating, we constructed chimeras of CIR and IRK1 and examined their electrophysiological properties. The channels were divided into three domains; the N-terminal cytoplasmic domain, the C-terminal cytoplasmic domain and the residual core domain. By the analysis, it was concluded that (i) the core region of CIR, but not the N and C cytoplasmic domains, is critical for the heteromultimer formation with GIRK1; and (ii) the N and C terminal cytoplasmic regions of CIR are sufficient for the G beta 1 gamma 2 gating. We also showed that the N terminal cytoplasmic region is involved in the determination of the rate of activation upon hyperpolarization.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/G Protein-Coupled...,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Kcnj5 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Muscarinic,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
3
|
pubmed:volume |
227
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
240-7
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8858132-Animals,
pubmed-meshheading:8858132-Biopolymers,
pubmed-meshheading:8858132-G Protein-Coupled Inwardly-Rectifying Potassium Channels,
pubmed-meshheading:8858132-GTP-Binding Proteins,
pubmed-meshheading:8858132-Ion Channel Gating,
pubmed-meshheading:8858132-Kinetics,
pubmed-meshheading:8858132-Myocardium,
pubmed-meshheading:8858132-Potassium Channels,
pubmed-meshheading:8858132-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:8858132-Rats,
pubmed-meshheading:8858132-Receptors, Muscarinic,
pubmed-meshheading:8858132-Recombinant Fusion Proteins,
pubmed-meshheading:8858132-Xenopus
|
pubmed:year |
1996
|
pubmed:articleTitle |
Identification of domains of the cardiac inward rectifying K+ channel, CIR, involved in the heteromultimer formation and in the G-protein gating.
|
pubmed:affiliation |
Department of Neurophysiology, Tokyo Metropolitan Institute for Neuroscience, Japan. ykubo@tmin.ac.jp
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|