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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2010-5-31
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pubmed:abstractText |
Neurotransmitter release and spontaneous action potentials during cochlear inner hair cell (IHC) development depend on the activity of Ca(v)1.3 voltage-gated L-type Ca(2+) channels. Their voltage- and Ca(2+)-dependent inactivation kinetics are slower than in other tissues but the underlying molecular mechanisms are not yet understood. We found that Rab3-interacting molecule-2alpha (RIM2alpha) mRNA is expressed in immature cochlear IHCs and the protein co-localizes with Ca(v)1.3 in the same presynaptic compartment of IHCs. Expression of RIM proteins in tsA-201 cells revealed binding to the beta-subunit of the channel complex and RIM-induced slowing of both Ca(2+)- and voltage-dependent inactivation of Ca(v)1.3 channels. By inhibiting inactivation, RIM induced a non-inactivating current component typical for IHC Ca(v)1.3 currents which should allow these channels to carry a substantial window current during prolonged depolarizations. These data suggest that RIM2 contributes to the stabilization of Ca(v)1.3 gating kinetics in immature IHCs.
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pubmed:grant |
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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 |
Jul
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pubmed:issn |
1095-9327
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pubmed:author |
pubmed-author:BrandtNielsN,
pubmed-author:EngelJuttaJ,
pubmed-author:GebhartMathiasM,
pubmed-author:Juhasz-VedresGabriellaG,
pubmed-author:KaurGurjotG,
pubmed-author:KnipperMarliesM,
pubmed-author:KoschakAlexandraA,
pubmed-author:ObermairGerald JGJ,
pubmed-author:StriessnigJörgJ,
pubmed-author:TrockenbacherAlexanderA,
pubmed-author:ZuccottiAnnalisaA
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pubmed:issnType |
Electronic
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
246-59
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pubmed:dateRevised |
2011-4-6
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pubmed:meshHeading |
pubmed-meshheading:20363327-Action Potentials,
pubmed-meshheading:20363327-Alternative Splicing,
pubmed-meshheading:20363327-Animals,
pubmed-meshheading:20363327-Calcium Channels, L-Type,
pubmed-meshheading:20363327-Cells, Cultured,
pubmed-meshheading:20363327-GTP-Binding Proteins,
pubmed-meshheading:20363327-Hair Cells, Auditory, Inner,
pubmed-meshheading:20363327-Humans,
pubmed-meshheading:20363327-Ion Channel Gating,
pubmed-meshheading:20363327-Mice,
pubmed-meshheading:20363327-Nerve Tissue Proteins,
pubmed-meshheading:20363327-Patch-Clamp Techniques,
pubmed-meshheading:20363327-Protein Isoforms,
pubmed-meshheading:20363327-Recombinant Fusion Proteins,
pubmed-meshheading:20363327-Two-Hybrid System Techniques,
pubmed-meshheading:20363327-rab3 GTP-Binding Proteins
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pubmed:year |
2010
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pubmed:articleTitle |
Modulation of Cav1.3 Ca2+ channel gating by Rab3 interacting molecule.
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pubmed:affiliation |
Institute of Pharmacy, Pharmacology and Toxicology, University of Innsbruck, Peter-Mayr-Strasse 1/I, A-6020 Innsbruck, Austria; Center of Molecular Biosciences Innsbruck (CMBI), Innsbruck, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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