English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

We investigated targeting mechanisms of Na +  and K ATP  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 I Na  and I KATP  functionally co-localize at the rat ICD, but not at the lateral membrane. Quantitative STORM imaging show that Na +  and K ATP  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 K ATP  channels to the ICD, but not to lateral membranes. Finally, a clinically relevant gene variant that disrupts K ATP  channel trafficking also regulates Na +  channel surface expression. The functional coupling between these two channels need to be considered when assessing clinical variants and therapeutics.

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