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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0026882,
umls-concept:C0185117,
umls-concept:C0205148,
umls-concept:C0225828,
umls-concept:C0678227,
umls-concept:C1142166,
umls-concept:C1167622,
umls-concept:C1412404,
umls-concept:C1419864,
umls-concept:C1533157,
umls-concept:C2911684
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pubmed:issue |
50
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pubmed:dateCreated |
2004-12-15
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pubmed:abstractText |
We identify a human mutation (E1053K) in the ankyrin-binding motif of Na(v)1.5 that is associated with Brugada syndrome, a fatal cardiac arrhythmia caused by altered function of Na(v)1.5. The E1053K mutation abolishes binding of Na(v)1.5 to ankyrin-G, and also prevents accumulation of Na(v)1.5 at cell surface sites in ventricular cardiomyocytes. Ankyrin-G and Na(v)1.5 are both localized at intercalated disc and T-tubule membranes in cardiomyocytes, and Na(v)1.5 coimmunoprecipitates with 190-kDa ankyrin-G from detergent-soluble lysates from rat heart. These data suggest that Na(v)1.5 associates with ankyrin-G and that ankyrin-G is required for Na(v)1.5 localization at excitable membranes in cardiomyocytes. Together with previous work in neurons, these results in cardiomyocytes suggest that ankyrin-G participates in a common pathway for localization of voltage-gated Na(v) channels at sites of function in multiple excitable cell types.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-11053140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-11273715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-11410597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-11724816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-11786529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-11796721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-11891345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-11901046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-11972032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-12478303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-12480819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-12571597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-12657669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-12716895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-12829783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-14597261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-14757759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-15042347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-2560390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-8989112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-9572267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-9664041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15579534-9832557
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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 |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
101
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17533-8
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pubmed:dateRevised |
2011-7-22
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pubmed:meshHeading |
pubmed-meshheading:15579534-Amino Acid Sequence,
pubmed-meshheading:15579534-Animals,
pubmed-meshheading:15579534-Ankyrins,
pubmed-meshheading:15579534-Cell Line,
pubmed-meshheading:15579534-Cell Membrane,
pubmed-meshheading:15579534-Gene Expression Regulation,
pubmed-meshheading:15579534-Glutamic Acid,
pubmed-meshheading:15579534-Humans,
pubmed-meshheading:15579534-Kinetics,
pubmed-meshheading:15579534-Mice,
pubmed-meshheading:15579534-Molecular Sequence Data,
pubmed-meshheading:15579534-Muscle Proteins,
pubmed-meshheading:15579534-Mutation, Missense,
pubmed-meshheading:15579534-Myocardium,
pubmed-meshheading:15579534-Myocytes, Cardiac,
pubmed-meshheading:15579534-Protein Binding,
pubmed-meshheading:15579534-Sodium Channels,
pubmed-meshheading:15579534-Syndrome
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pubmed:year |
2004
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pubmed:articleTitle |
Nav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Nav1.5 on the surface of cardiomyocytes.
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pubmed:affiliation |
Howard Hughes Medical Institute and Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA. peter.j.mohler@vanderbilt.edu
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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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