Linked Life Data

9245502

Source:http://linkedlifedata.com/resource/pubmed/id/9245502

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-10-27
pubmed:databankReference
pubmed:abstractText
Cardiac G protein-activated Kir (GIRK) channels may assemble as heterotetrameric polypeptides from two subunits, Kir3.1 and Kir3.4. For a functional comparison with native channels in the CNS we investigated all possible combinations of heteromeric channel formation from brain Kir3.1, Kir3.2, Kir3.3, and Kir3.4 subunits in mRNA-injected Xenopus oocytes. Analysis of macroscopic current amplitudes and channel gating kinetics indicated that individual subunits or combinations of Kir3.2, Kir3.3, and Kir3.4 formed functional channels ineffectively. Each of these subunits gave rise to prominent currents with distinct characteristics only in the presence of Kir3.1 subunits. Functional expression of concatemeric constructs between Kir3.1 and Kir3.2/3.4 subunits as well as coimmunoprecipitations with subunit-specific antibodies confirmed heteromeric channel formation. Mutational swapping between subunits of a single pore loop residue (Kir3.1F137S; Kir3.3S114F; a phenylalanine confers slow channel gating in Kir3.1 subunits) revealed that Kir3.1 subunits are an important constituent for native heteromeric channels and dominate their functional properties. However, homomeric channels from Kir3.1 subunits in vivo may not exist due to the spatial conflict of bulky phenylalanines in the pore structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1044-7431
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
194-206
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Subunit interactions in the assembly of neuronal Kir3.0 inwardly rectifying K+ channels.
pubmed:affiliation
Max-Planck-Institute for Biophysical Chemistry, Molecular Neurobiology of Signal Transduction, Göttingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't