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Ankyrin-G mediates targeting of both Na+ and KATP channels to the rat cardiac intercalated disc

Elife. 2020; 
Yang HQ, Pérez-Hernández M, Sanchez-Alonso J, Shevchuk A, Gorelik J, Rothenberg E, Delmar M, Coetzee WA,
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Molecular Biology Reagents source Designation Source or reference Identifiers Additional information Cell line (Homo-sapiens) HEK293 ATCC Cat# CRL-1573, RRID:CVCL_0045 Mycoplasma contamination negative Recombinant DNA reagent Nav1.5 Tan et al., 2018 Recombinant DNA reagent Kir6.2 Yang et al., 2018 Recombinant DNA reagent Kir6.2-myc Yang et al., 2018 Recombinant DNA reagent Avi-Kir6.2-myc Yang et al., 2018 Recombinant DNA reagent Kir6.2-KKK This paper Genscript Get A Quote

摘要

We investigated targeting mechanisms of Na+ and KATP channels to the intercalated disk (ICD) of cardiomyocytes. Patch clamp and surface biotinylation data show reciprocal downregulation of each other's surface density. Mutagenesis of the Kir6.2 ankyrin binding site disrupts this functional coupling. Duplex patch clamping and Angle SICM recordings show that INa and IKATP functionally co-localize at the rat ICD, but not at the lateral membrane. Quantitative STORM imaging show that Na+ and KATP channels are localized close to each other and to AnkG, but not to AnkB, at the ICD. Peptides corresponding to Nav1.5 and Kir6.2 ankyrin binding sites dysregulate targeting of both Na+ and KATP channels to the ICD, but not ... More

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