biostudies-literatureNguyen HMNINDS NIH HHS18577-82https://www.ebi.ac.uk/biostudies/studies/S-EPMC3494885biostudies-literatureUnknown109(45)Voltage-gated sodium (Na(V)) and potassium (K(V)) channels are critical components of neuronal action potential generation and propagation. Here, we report that Na(V)β1 encoded by SCN1b, an integral subunit of Na(V) channels, coassembles with and modulates the biophysical properties of K(V)1 and K(V)7 channels, but not K(V)3 channels, in an isoform-specific manner. Distinct domains of Na(V)β1 are involved in modulation of the different K(V) channels. Studies with channel chimeras demonstrate that Na(V)β1-mediated changes in activation kinetics and voltage dependence of activation require interaction of Na(V)β1 with the channel's voltage-sensing domain, whereas changes in inactivation and deactivation require interaction with the channel's pore domain. A molecular model based on docking stuProceedings of the National Academy of Sciences of the United States of AmericaModulation of voltage-gated K+ channels by the sodium channel β1 subunit.PMC3494885R01 NS048336R01 NS067288NS048336R01 NS048252NS48252NS067288Nukina NHoshi NNguyen HMChandy KGMiyazaki HGoldin ALSmith BJfalseModulation of voltage-gated K+ channels by the sodium channel β1 subunit.Voltage-gated sodium (Na(V)) and potassium (K(V)) channels are critical components of neuronal action potential generation and propagation. Here, we report that Na(V)β1 encoded by SCN1b, an integral subunit of Na(V) channels, coassembles with and modulates the biophysical properties of K(V)1 and K(V)7 channels, but not K(V)3 channels, in an isoform-specific manner. Distinct domains of Na(V)β1 are involved in modulation of the different K(V) channels. Studies with channel chimeras demonstrate that Na(V)β1-mediated changes in activation kinetics and voltage dependence of activation require interaction of Na(V)β1 with the channel's voltage-sensing domain, whereas changes in inactivation and deactivation require interaction with the channel's pore domain. A molecular model based on docking stu2012-01-01T00:00:00Z2012 Nov2025-04-04T10:11:36.166Z2019-03-27T01:00:17ZS-EPMC34948852309099010.1073/pnas.1209142109