β1-subunit–induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel

Castillo, Juan P., Sánchez-Rodríguez, Jorge E., Hyde, H. Clark, Zaelzer, Cristian A., Aguayo, Daniel, Sepúlveda, Romina V., Luk, Louis Y. P. ORCID: https://orcid.org/0000-0002-7864-6261, Kent, Stephen B. H., Gonzalez-Nilo, Fernando D., Bezanilla, Francisco and Latorre, Ramón 2016. β1-subunit–induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel. Proceedings of the National Academy of Sciences 113 (23) , E3231-E3239. 10.1073/pnas.1606381113

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Abstract

Large-conductance Ca2+- and voltage-activated K+ (BK) channels play many physiological roles, ranging from the maintenance of smooth muscle tone to the modulation of alcohol tolerance. In most cases, this physiological versatility of the BK channel is due to the association of the pore-forming α-subunit with β-subunits. Therefore, it is of importance to know what the structural consequences of this association are. Here, using lanthanide-based resonance energy transfer, we were able to determine the extracellular position of transmembrane segments S0–S2 with and without the β1-subunit and the position of the two transmembrane segments of the β1 subunit in the α/β1-subunit complex. We concluded that β1 produces rearrangements of the BK voltage sensor domain.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry
Subjects:	Q Science > QD Chemistry
Additional Information:	Pdf uploaded in accordance with publisher's policy at http://www.sherpa.ac.uk/romeo/issn/1091-6490/ (accessed 22/06/2016)
Publisher:	National Academy of Sciences
ISSN:	0027-8424
Date of First Compliant Deposit:	25 May 2016
Date of Acceptance:	26 April 2016
Last Modified:	18 Nov 2024 13:45
URI:	https://orca.cardiff.ac.uk/id/eprint/91217

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