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• W2000548245 abstract "Shaker-type potassium channels play important roles in determining the electrical excitability of cells. The native channel complex is thought to be formed by four pore-forming alpha subunits that provide four interaction sites for auxiliary modulatory Kvbeta subunits. Because Kvbeta subunits possess diverse modulatory activities including either up-regulation or down-regulation of potassium currents, differential assembly of the alpha-beta complex could give rise to diverse current properties. However, the detailed physical and functional stoichiometry of the alpha-beta complex remains unknown. Kvbeta1 subunits reduce potassium currents through inactivation, whereas Kvbeta2 subunits enhance potassium currents by inhibiting the Kvbeta1-mediated inactivation and at the same time by promoting the surface expression of certain potassium channels. In this report we show that Kvbeta1 and Kvbeta2 of the Shaker-type potassium channels display distinct functional stoichiometry to interact with the Kv1 alpha subunits, a subfamily of Shaker-type potassium channels. The interaction of Kvbeta1 subunits with alpha subunits is consistent with the alpha4betan model, where n equals 0, 1, 2, 3, or 4, depending upon the relative concentration of alpha and beta subunits. The alpha4betan stoichiometry allows for gradual changes of the Kvbeta1-mediated inactivation. In contrast, Kvbeta2 subunits self-associate to form oligomers and interact with the alpha subunits via alpha4beta4 stoichiometry, which permits effective multivalent associations with alpha subunits. Such distinct functional stoichiometry of Kvbeta1 and Kvbeta2 provides a molecular mechanism that is well suited to their contrasting activities of up-regulation or down-regulation of potassium currents." @default.
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• W2000548245 date "1998-02-17" @default.
• W2000548245 modified "2023-09-24" @default.
• W2000548245 title "Distinct functional stoichiometry of potassium channel β subunits" @default.
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• W2000548245 doi "https://doi.org/10.1073/pnas.95.4.1846" @default.
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