Statements in which the resource exists as a subject.
PredicateObject
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
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: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