Modulation of BK channel voltage gating by different auxiliary β subunits
Author
dc.contributor.author
Contreras, Gustavo F.
Author
dc.contributor.author
Neely, Alan
Author
dc.contributor.author
Alvarez, Osvaldo
Author
dc.contributor.author
Gonzalez, Carlos
Author
dc.contributor.author
Latorre, Ramón
Admission date
dc.date.accessioned
2019-03-15T16:03:28Z
Available date
dc.date.available
2019-03-15T16:03:28Z
Publication date
dc.date.issued
2012
Cita de ítem
dc.identifier.citation
Proceedings of the National Academy of Sciences of the United States of America, Volumen 109, Issue 46, 2018, Pages 18991-18996
Identifier
dc.identifier.issn
00278424
Identifier
dc.identifier.issn
10916490
Identifier
dc.identifier.other
10.1073/pnas.1216953109
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/165839
Abstract
dc.description.abstract
Calcium- and voltage-activated potassium channels (BK) are regulated by a multiplicity of signals. The prevailing view is that different BK gating mechanisms converge to determine channel opening and that these gating mechanisms are allosterically coupled. In most instances the pore forming α subunit of BK is associated with one of four alternative β subunits that appear to target specific gating mechanisms to regulate the channel activity. In particular, β1 stabilizes the active configuration of the BK voltage sensor having a large effect on BK Ca2+ sensitivity. To determine the extent to which β subunits regulate the BK voltage sensor, we measured gating currents induced by the pore-forming BK α subunit alone and with the different β subunits expressed in Xenopus oocytes (β1, β2IR, β3b, and β4). We found that β1, β2, and β4 stabilize the BK voltage sensor in the active conformation. β3 has no effect on voltage sensor equilibrium. In addition, β4 decreases the apparent number of charg