Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6542
|
| pubmed:dateCreated |
1995-9-22
|
| pubmed:databankReference | |
| pubmed:abstractText |
Potassium channels catalyse the permeation of K+ ions across cellular membranes and are identified by a common structural motif, a highly conserved signature sequence of eight amino acids in the P domain of each channel's pore-forming alpha-subunit. Here we describe a novel K+ channel (TOK1) from Saccharomyces cerevisiae that contains two P domains within one continuous polypeptide. Xenopus laevis oocytes expressing the channel exhibit a unique, outwardly rectifying, K(+)-selective current. The channel is permeable to outward flow of ions at membrane potentials above the K+ equilibrium potential; its conduction-voltage relationship is thus sensitive to extracellular K+ ion concentration. In excised membrane patches, external divalent cations block the channel in a voltage-dependent manner, and their removal in this configuration allows inward channel current. These attributes are similar to those described for inwardly rectifying K+ channels, but in the opposite direction, a previously unrecognized channel behaviour. Our results identify a new class of K+ channel which is distinctive in both its primary structure and functional properties. Structural homologues of the channel are present in the genome of Caenorhabditis elegans.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0028-0836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
|
| pubmed:volume |
376
|
| pubmed:geneSymbol |
TOK1
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
690-5
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7651518-Amino Acid Sequence,
pubmed-meshheading:7651518-Animals,
pubmed-meshheading:7651518-Base Sequence,
pubmed-meshheading:7651518-Caenorhabditis elegans,
pubmed-meshheading:7651518-Cells, Cultured,
pubmed-meshheading:7651518-DNA Primers,
pubmed-meshheading:7651518-Drosophila,
pubmed-meshheading:7651518-Molecular Sequence Data,
pubmed-meshheading:7651518-Oocytes,
pubmed-meshheading:7651518-Patch-Clamp Techniques,
pubmed-meshheading:7651518-Potassium,
pubmed-meshheading:7651518-Potassium Channels,
pubmed-meshheading:7651518-Protein Conformation,
pubmed-meshheading:7651518-Recombinant Proteins,
pubmed-meshheading:7651518-Saccharomyces cerevisiae,
pubmed-meshheading:7651518-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:7651518-Sequence Homology, Amino Acid,
pubmed-meshheading:7651518-Sodium,
pubmed-meshheading:7651518-Xenopus laevis
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem.
|
| pubmed:affiliation |
Department of Pediatrics, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06536-0812, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|