{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tedeschi G"],"funding":["NIDCD NIH HHS","National Institutes of Health, National Institute of General Medicine","National Institutes of Health","NIGMS NIH HHS"],"pagination":["10719"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8140153"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_abstract":["Voltage-gated potassium (Kv) channels are a family of membrane proteins that facilitate K<sup>+</sup> 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 KCN"],"journal":["Scientific reports"],"pubmed_title":["Fluorescence Fluctuation Spectroscopy enables quantification of potassium channel subunit dynamics and stoichiometry."],"pmcid":["PMC8140153"],"funding_grant_id":["P41 GM103540","R21 DC015736","R21DC015736","8P41-GM103540"],"pubmed_authors":["Papanikolaou M","Abbott GW","Digman MA","Scipioni L","Tedeschi G"],"additional_accession":[]},"is_claimable":false,"name":"Fluorescence Fluctuation Spectroscopy enables quantification of potassium channel subunit dynamics and stoichiometry.","description":"Voltage-gated potassium (Kv) channels are a family of membrane proteins that facilitate K<sup>+</sup> 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 KCN","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 May","modification":"2025-04-04T07:22:36.611Z","creation":"2025-04-04T07:22:36.611Z"},"accession":"S-EPMC8140153","cross_references":{"pubmed":["34021177"],"doi":["10.1038/s41598-021-90002-2"]}}