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- W3111041204 abstract "Voltage-gated potassium (Kv) channels are a family of membrane proteins that facilitate K+ ion diffusion across the plasma membrane, regulating both resting and action potentials. Kv channels comprise four pore-forming α subunits, each with a voltage sensing domain, and they are regulated by interaction with β subunits such as those belonging to the KCNE family. Here we conducted a comprehensive biophysical characterization of stoichiometry and protein diffusion across the plasma membrane of the epithelial KCNQ1-KCNE2 complex, combining total internal reflection fluorescence (TIRF) microscopy and a series of complementary Fluorescence Fluctuation Spectroscopy (FFS) techniques. Using this approach, we found that KCNQ1-KCNE2 has a predominant 4:4 stoichiometry, while non-bound KCNE2 subunits are mostly present as dimers in the plasma membrane. At the same time, we identified unique spatio-temporal diffusion modalities and nano-environment organization for each channel subunit. These findings improve our understanding of KCNQ1-KCNE2 channel function and suggest strategies for elucidating the subunit stoichiometry and forces directing localization and diffusion of ion channel complexes in general." @default.
- W3111041204 created "2020-12-21" @default.
- W3111041204 creator A5022236028 @default.
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- W3111041204 creator A5023372690 @default.
- W3111041204 creator A5062051181 @default.
- W3111041204 creator A5089995652 @default.
- W3111041204 date "2021-05-21" @default.
- W3111041204 modified "2023-10-14" @default.
- W3111041204 title "Fluorescence Fluctuation Spectroscopy enables quantification of potassium channel subunit dynamics and stoichiometry" @default.
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- W3111041204 doi "https://doi.org/10.1038/s41598-021-90002-2" @default.
- W3111041204 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8140153" @default.
- W3111041204 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34021177" @default.
- W3111041204 hasPublicationYear "2021" @default.
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