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: Contribución a la publicaciónArticle

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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
Número de edición23
Identificadores de objetos digitales
EstadoPublished - 7 jun 2016

Huella dactilar

Large-Conductance Calcium-Activated Potassium Channels
Lanthanoid Series Elements
Energy Transfer
Terbium

Keywords

    ASJC Scopus subject areas

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    Castillo, J. P., Sánchez-Rodríguez, J. E., Hyde, H. C., Zaelzer, C. A., Aguayo, D., Sepúlveda, R. V., ... 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, 113(23), E3231-E3239. DOI: 10.1073/pnas.1606381113

    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, Vol. 113, N.º 23, 07.06.2016, p. E3231-E3239.

    Resultado de la investigación: Contribución a la publicaciónArticle

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    title = "β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel",
    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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    author = "Castillo, {Juan P.} and Sánchez-Rodríguez, {Jorge E.} and Hyde, {H. Clark} and Zaelzer, {Cristian A.} and Daniel Aguayo and Sepúlveda, {Romina V.} and Luk, {Louis Y P} and Kent, {Stephen B H} and Gonzalez-Nilo, {Fernando D.} and Francisco Bezanilla and Ramón Latorre",
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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. DOI: 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: Contribución a la publicaciónArticle

    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

    VL - 113

    SP - E3231-E3239

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

    T2 - 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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    Castillo JP, Sánchez-Rodríguez JE, Hyde HC, Zaelzer CA, Aguayo D, Sepúlveda RV y otros. 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. 2016 jun 7;113(23):E3231-E3239. Disponible desde, DOI: 10.1073/pnas.1606381113