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

Juan P. Castillo, Jorge E. Sánchez-Rodríguez, H. Clark Hyde, Cristian A. Zaelzer, Daniel Aguayo, Romina V. Sepúlveda, Louis Y P Luk, Stephen B H Kent, Fernando D. Gonzalez-Nilo, Francisco Bezanilla, Ramón Latorre

Resultado de la investigación: Article

11 Citas (Scopus)

Resumen

Large-conductance Ca2+- and voltage-activated K+ (BK) channels are involved in a large variety of physiological processes. Regulatory β-subunits are one of the mechanisms responsible for creating BK channel diversity fundamental to the adequate function of many tissues. However, little is known about the structure of its voltage sensor domain. Here, we present the external architectural details of BK channels using lanthanide-based resonance energy transfer (LRET). We used a genetically encoded lanthanide-binding tag (LBT) to bind terbium as a LRET donor and a fluorophore-labeled iberiotoxin as the LRET acceptor for measurements of distances within the BK channel structure in a living cell. By introducing LBTs in the extracellular region of the α- or β1-subunit, we determined (i) a basic extracellular map of the BK channel, (ii) β1-subunit-induced rearrangements of the voltage sensor in α-subunits, and (iii) the relative position of the β1-subunit within the α/β1-subunit complex.

Idioma originalEnglish
Páginas (desde-hasta)E3231-E3239
PublicaciónProceedings of the National Academy of Sciences of the United States of America
Volumen113
N.º23
DOI
EstadoPublished - 7 jun 2016

Huella dactilar

electric potential
energy transfer
terbium
sensors

ASJC Scopus subject areas

  • General

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Castillo, Juan P. ; Sánchez-Rodríguez, Jorge E. ; Hyde, H. Clark ; Zaelzer, Cristian A. ; Aguayo, Daniel ; Sepúlveda, Romina V. ; Luk, Louis Y P ; Kent, Stephen B H ; Gonzalez-Nilo, Fernando D. ; Bezanilla, Francisco ; Latorre, Ramón. / β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel. En: Proceedings of the National Academy of Sciences of the United States of America. 2016 ; Vol. 113, N.º 23. pp. E3231-E3239.
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abstract = "Large-conductance Ca2+- and voltage-activated K+ (BK) channels are involved in a large variety of physiological processes. Regulatory β-subunits are one of the mechanisms responsible for creating BK channel diversity fundamental to the adequate function of many tissues. However, little is known about the structure of its voltage sensor domain. Here, we present the external architectural details of BK channels using lanthanide-based resonance energy transfer (LRET). We used a genetically encoded lanthanide-binding tag (LBT) to bind terbium as a LRET donor and a fluorophore-labeled iberiotoxin as the LRET acceptor for measurements of distances within the BK channel structure in a living cell. By introducing LBTs in the extracellular region of the α- or β1-subunit, we determined (i) a basic extracellular map of the BK channel, (ii) β1-subunit-induced rearrangements of the voltage sensor in α-subunits, and (iii) the relative position of the β1-subunit within the α/β1-subunit complex.",
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Castillo, JP, Sánchez-Rodríguez, JE, Hyde, HC, Zaelzer, CA, Aguayo, D, Sepúlveda, RV, Luk, LYP, Kent, SBH, Gonzalez-Nilo, FD, Bezanilla, F & Latorre, R 2016, 'β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel', Proceedings of the National Academy of Sciences of the United States of America, vol. 113, n.º 23, pp. E3231-E3239. https://doi.org/10.1073/pnas.1606381113

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; Kent, Stephen B H; Gonzalez-Nilo, Fernando D.; Bezanilla, Francisco; Latorre, Ramón.

En: Proceedings of the National Academy of Sciences of the United States of America, Vol. 113, N.º 23, 07.06.2016, p. E3231-E3239.

Resultado de la investigación: Article

TY - JOUR

T1 - β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel

AU - Castillo, Juan P.

AU - Sánchez-Rodríguez, Jorge E.

AU - Hyde, H. Clark

AU - Zaelzer, Cristian A.

AU - Aguayo, Daniel

AU - Sepúlveda, Romina V.

AU - Luk, Louis Y P

AU - Kent, Stephen B H

AU - Gonzalez-Nilo, Fernando D.

AU - Bezanilla, Francisco

AU - Latorre, Ramón

PY - 2016/6/7

Y1 - 2016/6/7

N2 - Large-conductance Ca2+- and voltage-activated K+ (BK) channels are involved in a large variety of physiological processes. Regulatory β-subunits are one of the mechanisms responsible for creating BK channel diversity fundamental to the adequate function of many tissues. However, little is known about the structure of its voltage sensor domain. Here, we present the external architectural details of BK channels using lanthanide-based resonance energy transfer (LRET). We used a genetically encoded lanthanide-binding tag (LBT) to bind terbium as a LRET donor and a fluorophore-labeled iberiotoxin as the LRET acceptor for measurements of distances within the BK channel structure in a living cell. By introducing LBTs in the extracellular region of the α- or β1-subunit, we determined (i) a basic extracellular map of the BK channel, (ii) β1-subunit-induced rearrangements of the voltage sensor in α-subunits, and (iii) the relative position of the β1-subunit within the α/β1-subunit complex.

AB - Large-conductance Ca2+- and voltage-activated K+ (BK) channels are involved in a large variety of physiological processes. Regulatory β-subunits are one of the mechanisms responsible for creating BK channel diversity fundamental to the adequate function of many tissues. However, little is known about the structure of its voltage sensor domain. Here, we present the external architectural details of BK channels using lanthanide-based resonance energy transfer (LRET). We used a genetically encoded lanthanide-binding tag (LBT) to bind terbium as a LRET donor and a fluorophore-labeled iberiotoxin as the LRET acceptor for measurements of distances within the BK channel structure in a living cell. By introducing LBTs in the extracellular region of the α- or β1-subunit, we determined (i) a basic extracellular map of the BK channel, (ii) β1-subunit-induced rearrangements of the voltage sensor in α-subunits, and (iii) the relative position of the β1-subunit within the α/β1-subunit complex.

KW - BK channels

KW - Lanthanide resonance energy transfer

KW - β 1-subunit

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U2 - 10.1073/pnas.1606381113

DO - 10.1073/pnas.1606381113

M3 - Article

AN - SCOPUS:84973316259

VL - 113

SP - E3231-E3239

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

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ER -