| http://purl.uniprot.org/citations/21084288 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21084288 | http://www.w3.org/2000/01/rdf-schema#comment | "Voltage-gated T-type Ca(2+) channel Ca(v)3.2 (α(1H)) subunit, responsible for T-type Ca(2+) current, is expressed in different tissues and participates in Ca(2+) entry, hormonal secretion, pacemaker activity, and arrhythmia. The precise subcellular localization and regulation of Ca(v)3.2 channels in native cells is unknown. Caveolae containing scaffolding protein caveolin-3 (Cav-3) localize many ion channels, signaling proteins and provide temporal and spatial regulation of intracellular Ca(2+) in different cells. We examined the localization and regulation of the Ca(v)3.2 channels in cardiomyocytes. Immunogold labeling and electron microscopy analysis demonstrated co-localization of the Ca(v)3.2 channel and Cav-3 relative to caveolae in ventricular myocytes. Co-immunoprecipitation from neonatal ventricular myocytes or transiently transfected HEK293 cells demonstrated that Ca(v)3.1 and Ca(v)3.2 channels co-immunoprecipitate with Cav-3. GST pulldown analysis confirmed that the N terminus region of Cav-3 closely interacts with Ca(v)3.2 channels. Whole cell patch clamp analysis demonstrated that co-expression of Cav-3 significantly decreased the peak Ca(v)3.2 current density in HEK293 cells, whereas co-expression of Cav-3 did not alter peak Ca(v)3.1 current density. In neonatal mouse ventricular myocytes, overexpression of Cav-3 inhibited the peak T-type calcium current (I(Ca,T)) and adenovirus (AdCa(v)3.2)-mediated increase in peak Ca(v)3.2 current, but did not affect the L-type current. The protein kinase A-dependent stimulation of I(Ca,T) by 8-Br-cAMP (membrane permeable cAMP analog) was abolished by siRNA directed against Cav-3. Our findings on functional modulation of the Ca(v)3.2 channels by Cav-3 is important for understanding the compartmentalized regulation of Ca(2+) signaling during normal and pathological processes."xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.182550"xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/author | "Balijepalli R.C."xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/author | "Cribbs L.L."xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/author | "Pluteanu F."xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/author | "Fahey J.M."xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/author | "Markandeya Y.S."xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/pages | "2433-2444"xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/title | "Caveolin-3 regulates protein kinase A modulation of the Ca(V)3.2 (alpha1H) T-type Ca2+ channels."xsd:string |
| http://purl.uniprot.org/citations/21084288 | http://purl.uniprot.org/core/volume | "286"xsd:string |
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