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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2001-6-6
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pubmed:abstractText |
The interaction between the amino terminus of Kv1-type potassium channels and alpha-actinin-2 has been investigated. Using a combination of yeast two-hybrid analysis and in vitro binding assays, alpha-actinin-2 was found to bind to the N-termini of both Kv1.4 and Kv1.5 but not to the equivalent segments of Kv1.1, Kv1.2 or Kv1.3. Deletion analysis in the in vitro binding assays delineated the actinin binding region of Kv1.5 to between amino acids 73 and 148 of the channel. The Kv1.5 binding sites in alpha-actinin-2 were found to lie within actinin's internal spectrin repeats. Unlike the reported interaction between actinin and the NMDA receptor, calmodulin was found to have no effect on actinin binding to Kv1.5.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Actinin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Kv1.1 Potassium Channel,
http://linkedlifedata.com/resource/pubmed/chemical/Kv1.2 Potassium Channel,
http://linkedlifedata.com/resource/pubmed/chemical/Kv1.3 Potassium Channel,
http://linkedlifedata.com/resource/pubmed/chemical/Kv1.4 Potassium Channel,
http://linkedlifedata.com/resource/pubmed/chemical/Kv1.5 Potassium Channel,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Voltage-Gated,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Spectrin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
498
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
87-92
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11389904-Actinin,
pubmed-meshheading:11389904-Binding Sites,
pubmed-meshheading:11389904-Calcium,
pubmed-meshheading:11389904-Calmodulin,
pubmed-meshheading:11389904-Escherichia coli,
pubmed-meshheading:11389904-Kv1.1 Potassium Channel,
pubmed-meshheading:11389904-Kv1.2 Potassium Channel,
pubmed-meshheading:11389904-Kv1.3 Potassium Channel,
pubmed-meshheading:11389904-Kv1.4 Potassium Channel,
pubmed-meshheading:11389904-Kv1.5 Potassium Channel,
pubmed-meshheading:11389904-Molecular Sequence Data,
pubmed-meshheading:11389904-Potassium Channels,
pubmed-meshheading:11389904-Potassium Channels, Voltage-Gated,
pubmed-meshheading:11389904-Protein Structure, Tertiary,
pubmed-meshheading:11389904-Recombinant Proteins,
pubmed-meshheading:11389904-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:11389904-Sequence Homology, Amino Acid,
pubmed-meshheading:11389904-Spectrin
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pubmed:year |
2001
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pubmed:articleTitle |
A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2.
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pubmed:affiliation |
Department of Physiology, University of British Columbia, Vancouver, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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