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- W806183961 abstract "KCNE peptides are a class of type I transmembrane β-subunits that assemble with and modulate the gating and ion conducting properties of a variety of voltage-gated K channels. Accordingly, mutations that disrupt the assembly and trafficking of KCNE-K channel complexes give rise to disease. The cellular mechanisms responsible for ensuring that KCNE peptides assemble with voltage-gated K channels have yet to be elucidated. Using enzymatic deglycosylation, immunofluorescence, and quantitative cell surface labeling experiments, we show that KCNE1 (E1) peptides are retained in the early stages of the secretory pathway until they co-assemble with specific K channel subunits; coassembly mediates E1 progression through the secretory pathway and results in cell surface expression. We also address an apparent discrepancy between our results and a previous study in human embryonic kidney cells, which showed wild type E1 peptides can reach the plasma membrane without exogenously expressed K channel subunits. By comparing E1 trafficking in three cell lines, our data suggest that the errant E1 trafficking observed in human embryonic kidney cells may be due, in part, to the presence of endogenous voltage-gated K channels in these cells." @default.
- W806183961 created "2016-06-24" @default.
- W806183961 creator A5081996257 @default.
- W806183961 date "2010-01-01" @default.
- W806183961 modified "2023-10-03" @default.
- W806183961 title "Glycosylation, Assembly and Trafficking of Cardiac Potassium Channel Complexes: A Dissertation" @default.
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