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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1993-2-10
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pubmed:abstractText |
Shaker K+ channels are multimeric, probably tetrameric proteins. Substitution of a conserved leucine residue to valine (V2) at position 370 in the Drosophila Shaker 29-4 sequence results in large alterations in the voltage dependence of gating in the expressed channels. In order to determine the effects of this mutation in hybrid channels with a fixed stoichiometry of V2 and wild-type (WT) subunits we generated cDNA constructs of two linked-monomeric subunits similar to the tandem constructs previously reported by Isacoff, E. Y., Y. N. Jan, and L. Y. Jan. (1990. Nature (Lond.). 345:530-534). In addition, we constructed a tandem cDNA containing a wild-type subunit and a truncated nonfunctional subunit (Sh102) that suppresses channel expression. We report that the voltage-dependence of the channels produced with WT and V2 subunits varied significantly with the order of the subunits in the construct (WT-V2 or V2-WT), while the WT-Sh102 construct yielded currents that were much larger than expected. These results suggest that the tandem linkage of Shaker subunits does not guarantee the stoichiometry of the expressed channel proteins.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-1370654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-1550673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-1550674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-1553560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-1697898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-1699527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-1706481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-1899917,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2000494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2000495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2011602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2112229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2122519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2201450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2317379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2348860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2369521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2412759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2459775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2551680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-2688707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-3272175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-3272184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1477286-7198941
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1406-11
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1477286-Amino Acid Sequence,
pubmed-meshheading:1477286-Animals,
pubmed-meshheading:1477286-Biophysical Phenomena,
pubmed-meshheading:1477286-Biophysics,
pubmed-meshheading:1477286-Cloning, Molecular,
pubmed-meshheading:1477286-DNA,
pubmed-meshheading:1477286-Drosophila,
pubmed-meshheading:1477286-Electrochemistry,
pubmed-meshheading:1477286-Female,
pubmed-meshheading:1477286-Molecular Sequence Data,
pubmed-meshheading:1477286-Mutagenesis, Site-Directed,
pubmed-meshheading:1477286-Oocytes,
pubmed-meshheading:1477286-Potassium Channels,
pubmed-meshheading:1477286-Protein Conformation,
pubmed-meshheading:1477286-Xenopus
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pubmed:year |
1992
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pubmed:articleTitle |
Tandem linkage of Shaker K+ channel subunits does not ensure the stoichiometry of expressed channels.
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pubmed:affiliation |
Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06510.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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