Structural determinants for functional coupling between the β and α subunits in the Ca2+-activated K+ (BK) channel
Author
dc.contributor.author
Orio, Patricio
Author
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Torres, Yolima
Author
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Rojas, Patricio
Author
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Carvacho, Ingrid
Author
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Garcia, Maria L.
Author
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Toro, Ligia
Author
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Valverde, Miguel A.
Author
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Latorre, Ramón
Admission date
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2019-01-29T17:57:16Z
Available date
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2019-01-29T17:57:16Z
Publication date
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2006
Cita de ítem
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Journal of General Physiology, Volumen 127, Issue 2, 2018, Pages 191-204
Identifier
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00221295
Identifier
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00221295
Identifier
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10.1085/jgp.200509370
Identifier
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https://repositorio.uchile.cl/handle/2250/163974
Abstract
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High conductance, calcium- and voltage-activated potassium (BK, MaxiK) channels are widely expressed in mammals. In some tissues, the biophysical properties of BK channels are highly affected by coexpression of regulatory (β) subunits. The most remarkable effects of β1 and β2 subunits are an increase of the calcium sensitivity and the slow down of channel kinetics. However, the detailed characteristics of channels formed by α and β1 or β2 are dissimilar, the most remarkable difference being a reduction of the voltage sensitivity in the presence of β1 but not β2. Here we reveal the molecular regions in these β subunits that determine their differential functional coupling with the pore-forming α-subunit. We made chimeric constructs between β1 and β2 subunits, and BK channels formed by α and chimeric β subunits were expressed in Xenopus laevis oocytes. The electrophysiological characteristics of the resulting channels were determined using the patch clamp technique. Chimeric exchange of