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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 2
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pubmed:dateCreated |
2005-10-17
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pubmed:abstractText |
Association of Shal gene-related voltage-gated potassium (Kv4) channels with cytoplasmic Kv channel interacting proteins (KChIPs) influences inactivation gating and surface expression. We investigated both functional and biochemical consequences of mutations in cytoplasmic N and C-terminal Kv4.2 domains to characterize structural determinants for KChIP interaction. We performed a lysine-scanning mutagenesis within the proximal 40 amino acid portion and a structure-based mutagenesis in the tetramerization 1 (T1) domain of Kv4.2. In addition, the cytoplasmic Kv4.2 C-terminus was truncated at various positions. Wild-type and mutant Kv4.2 channels were coexpressed with KChIP2 isoforms in mammalian cell lines. The KChIP2-induced modulation of Kv4.2 currents was studied with whole-cell patch clamp and the binding of KChIP2 isoforms to Kv4.2 channels with coimmunoprecipitation experiments. Our results define one major interaction site for KChIPs, including amino acids in the proximal N-terminus between residues 11 and 23, where binding and functional modulation are essentially equivalent. A further interaction site includes residues in the T1 domain. Notably, C-terminal deletions also had marked effects on KChIP2-dependent gating modulation and KChIP2 binding, revealing a previously unknown involvement of domains within the cytoplasmic Kv4.2 C-terminus in KChIP interaction. Less coincidence of binding and functional modulation indicates a more loose 'anchoring' at T1- and C-terminal interaction sites. Our results refine and extend previously proposed structural models for Kv4.2/KChIP complex formation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-10551270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-10676964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-10884227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-11115393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-11287421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-11323678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-11535596,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-11747815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-11826158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-11976919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-12006572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-12560340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-12575952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-12829703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-12835418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-12928444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-14623880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-14695263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-14980201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-14980206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-14980207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-15485870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-7823083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-8831489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16096338-8994601
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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 |
Oct
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pubmed:issn |
0022-3751
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
568
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
397-412
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16096338-Animals,
pubmed-meshheading:16096338-Binding Sites,
pubmed-meshheading:16096338-CHO Cells,
pubmed-meshheading:16096338-Cricetinae,
pubmed-meshheading:16096338-Cricetulus,
pubmed-meshheading:16096338-DNA Mutational Analysis,
pubmed-meshheading:16096338-Female,
pubmed-meshheading:16096338-Humans,
pubmed-meshheading:16096338-Ion Channel Gating,
pubmed-meshheading:16096338-Kv Channel-Interacting Proteins,
pubmed-meshheading:16096338-Membrane Potentials,
pubmed-meshheading:16096338-Mutagenesis, Site-Directed,
pubmed-meshheading:16096338-Patch-Clamp Techniques,
pubmed-meshheading:16096338-Protein Conformation,
pubmed-meshheading:16096338-Protein Structure, Tertiary,
pubmed-meshheading:16096338-Shal Potassium Channels,
pubmed-meshheading:16096338-Transfection
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pubmed:year |
2005
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pubmed:articleTitle |
Contribution of N- and C-terminal Kv4.2 channel domains to KChIP interaction [corrected].
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pubmed:affiliation |
Institut für Neurale Signalverarbeitung, Zentrum für Molekulare Neurobiologie Hamburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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