A BK (Slo1) channel journey from molecule to physiology
- Autores
- Contreras, Gustavo F.; Castillo, Karen Noel; Enrique, Nicolás Jorge; Carrasquel Ursulaez, William; Castillo, Juan Pablo; Milesi, Verónica; Neely, Allan; Alvarez, Osvaldo; Ferreira, Gonzalo; Gonzáez, Carlos; Latorre, Ramón
- Año de publicación
- 2013
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Calcium and voltage-activated potassium (BK) channels are key actors in cell physiology, both in neuronal and nonneuronal cells and tissues. Through negative feedback between intracellular Ca2+ and membrane voltage, BK channels provide a damping mechanism for excitatory signals. Molecular modulation of these channels by alternative splicing, auxiliary subunits and post-translational modifications showed that these channels are subjected to many mechanisms that add diversity to the BK channel α subunit gene. This complexity of interactions modulates BK channel gating, modifying the energetic barrier of voltage sensor domain activation and channel opening. Regions for voltage as well as Ca2+ sensitivity have been identified, and the crystal structure generated by the 2 RCK domains contained in the C-terminal of the channel has been described. The linkage of these channels to many intracellular metabolites and pathways, as well as their modulation by extracellular natural agents, has been found to be relevant in many physiological processes. This review includes the hallmarks of BK channel biophysics and its physiological impact on specific cells and tissues, highlighting its relationship with auxiliary subunit expression.
Fil: Contreras, Gustavo F.. Universidad de Valparaíso; Chile
Fil: Castillo, Karen Noel. Universidad de Valparaíso; Chile
Fil: Enrique, Nicolás Jorge. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Grupo de Investigación en Fisiología Vascular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Carrasquel Ursulaez, William. Universidad de Valparaíso; Chile
Fil: Castillo, Juan Pablo. Universidad de Valparaíso; Chile. Universidad de Chile; Chile
Fil: Milesi, Verónica. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Grupo de Investigación en Fisiología Vascular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Neely, Allan. Universidad de Valparaíso; Chile
Fil: Alvarez, Osvaldo. Universidad de Chile; Chile
Fil: Ferreira, Gonzalo. Universidad de la República; Uruguay
Fil: Gonzáez, Carlos. Universidad de Valparaíso; Chile
Fil: Latorre, Ramón. Universidad de Valparaíso; Chile - Materia
-
Bk Channels
Slo1
Auxiliary Subunits
Voltage Sensor
Intracellular Ca2+
Smooth Muscle
Diseases - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/23668
Ver los metadatos del registro completo
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A BK (Slo1) channel journey from molecule to physiologyContreras, Gustavo F.Castillo, Karen NoelEnrique, Nicolás JorgeCarrasquel Ursulaez, WilliamCastillo, Juan PabloMilesi, VerónicaNeely, AllanAlvarez, OsvaldoFerreira, GonzaloGonzáez, CarlosLatorre, RamónBk ChannelsSlo1Auxiliary SubunitsVoltage SensorIntracellular Ca2+Smooth MuscleDiseaseshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Calcium and voltage-activated potassium (BK) channels are key actors in cell physiology, both in neuronal and nonneuronal cells and tissues. Through negative feedback between intracellular Ca2+ and membrane voltage, BK channels provide a damping mechanism for excitatory signals. Molecular modulation of these channels by alternative splicing, auxiliary subunits and post-translational modifications showed that these channels are subjected to many mechanisms that add diversity to the BK channel α subunit gene. This complexity of interactions modulates BK channel gating, modifying the energetic barrier of voltage sensor domain activation and channel opening. Regions for voltage as well as Ca2+ sensitivity have been identified, and the crystal structure generated by the 2 RCK domains contained in the C-terminal of the channel has been described. The linkage of these channels to many intracellular metabolites and pathways, as well as their modulation by extracellular natural agents, has been found to be relevant in many physiological processes. This review includes the hallmarks of BK channel biophysics and its physiological impact on specific cells and tissues, highlighting its relationship with auxiliary subunit expression.Fil: Contreras, Gustavo F.. Universidad de Valparaíso; ChileFil: Castillo, Karen Noel. Universidad de Valparaíso; ChileFil: Enrique, Nicolás Jorge. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Grupo de Investigación en Fisiología Vascular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Carrasquel Ursulaez, William. Universidad de Valparaíso; ChileFil: Castillo, Juan Pablo. Universidad de Valparaíso; Chile. Universidad de Chile; ChileFil: Milesi, Verónica. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Grupo de Investigación en Fisiología Vascular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Neely, Allan. Universidad de Valparaíso; ChileFil: Alvarez, Osvaldo. Universidad de Chile; ChileFil: Ferreira, Gonzalo. Universidad de la República; UruguayFil: Gonzáez, Carlos. Universidad de Valparaíso; ChileFil: Latorre, Ramón. Universidad de Valparaíso; ChileTaylor & Francis2013-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/23668Contreras, Gustavo F.; Castillo, Karen Noel; Enrique, Nicolás Jorge; Carrasquel Ursulaez, William; Castillo, Juan Pablo; et al.; A BK (Slo1) channel journey from molecule to physiology; Taylor & Francis; Channels; 7; 6; 9-2013; 442-4581933-6950CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.tandfonline.com/doi/abs/10.4161/chan.26242info:eu-repo/semantics/altIdentifier/doi/10.4161/chan.26242info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:37:04Zoai:ri.conicet.gov.ar:11336/23668instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:37:04.765CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
A BK (Slo1) channel journey from molecule to physiology |
title |
A BK (Slo1) channel journey from molecule to physiology |
spellingShingle |
A BK (Slo1) channel journey from molecule to physiology Contreras, Gustavo F. Bk Channels Slo1 Auxiliary Subunits Voltage Sensor Intracellular Ca2+ Smooth Muscle Diseases |
title_short |
A BK (Slo1) channel journey from molecule to physiology |
title_full |
A BK (Slo1) channel journey from molecule to physiology |
title_fullStr |
A BK (Slo1) channel journey from molecule to physiology |
title_full_unstemmed |
A BK (Slo1) channel journey from molecule to physiology |
title_sort |
A BK (Slo1) channel journey from molecule to physiology |
dc.creator.none.fl_str_mv |
Contreras, Gustavo F. Castillo, Karen Noel Enrique, Nicolás Jorge Carrasquel Ursulaez, William Castillo, Juan Pablo Milesi, Verónica Neely, Allan Alvarez, Osvaldo Ferreira, Gonzalo Gonzáez, Carlos Latorre, Ramón |
author |
Contreras, Gustavo F. |
author_facet |
Contreras, Gustavo F. Castillo, Karen Noel Enrique, Nicolás Jorge Carrasquel Ursulaez, William Castillo, Juan Pablo Milesi, Verónica Neely, Allan Alvarez, Osvaldo Ferreira, Gonzalo Gonzáez, Carlos Latorre, Ramón |
author_role |
author |
author2 |
Castillo, Karen Noel Enrique, Nicolás Jorge Carrasquel Ursulaez, William Castillo, Juan Pablo Milesi, Verónica Neely, Allan Alvarez, Osvaldo Ferreira, Gonzalo Gonzáez, Carlos Latorre, Ramón |
author2_role |
author author author author author author author author author author |
dc.subject.none.fl_str_mv |
Bk Channels Slo1 Auxiliary Subunits Voltage Sensor Intracellular Ca2+ Smooth Muscle Diseases |
topic |
Bk Channels Slo1 Auxiliary Subunits Voltage Sensor Intracellular Ca2+ Smooth Muscle Diseases |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Calcium and voltage-activated potassium (BK) channels are key actors in cell physiology, both in neuronal and nonneuronal cells and tissues. Through negative feedback between intracellular Ca2+ and membrane voltage, BK channels provide a damping mechanism for excitatory signals. Molecular modulation of these channels by alternative splicing, auxiliary subunits and post-translational modifications showed that these channels are subjected to many mechanisms that add diversity to the BK channel α subunit gene. This complexity of interactions modulates BK channel gating, modifying the energetic barrier of voltage sensor domain activation and channel opening. Regions for voltage as well as Ca2+ sensitivity have been identified, and the crystal structure generated by the 2 RCK domains contained in the C-terminal of the channel has been described. The linkage of these channels to many intracellular metabolites and pathways, as well as their modulation by extracellular natural agents, has been found to be relevant in many physiological processes. This review includes the hallmarks of BK channel biophysics and its physiological impact on specific cells and tissues, highlighting its relationship with auxiliary subunit expression. Fil: Contreras, Gustavo F.. Universidad de Valparaíso; Chile Fil: Castillo, Karen Noel. Universidad de Valparaíso; Chile Fil: Enrique, Nicolás Jorge. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Grupo de Investigación en Fisiología Vascular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Carrasquel Ursulaez, William. Universidad de Valparaíso; Chile Fil: Castillo, Juan Pablo. Universidad de Valparaíso; Chile. Universidad de Chile; Chile Fil: Milesi, Verónica. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Grupo de Investigación en Fisiología Vascular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Neely, Allan. Universidad de Valparaíso; Chile Fil: Alvarez, Osvaldo. Universidad de Chile; Chile Fil: Ferreira, Gonzalo. Universidad de la República; Uruguay Fil: Gonzáez, Carlos. Universidad de Valparaíso; Chile Fil: Latorre, Ramón. Universidad de Valparaíso; Chile |
description |
Calcium and voltage-activated potassium (BK) channels are key actors in cell physiology, both in neuronal and nonneuronal cells and tissues. Through negative feedback between intracellular Ca2+ and membrane voltage, BK channels provide a damping mechanism for excitatory signals. Molecular modulation of these channels by alternative splicing, auxiliary subunits and post-translational modifications showed that these channels are subjected to many mechanisms that add diversity to the BK channel α subunit gene. This complexity of interactions modulates BK channel gating, modifying the energetic barrier of voltage sensor domain activation and channel opening. Regions for voltage as well as Ca2+ sensitivity have been identified, and the crystal structure generated by the 2 RCK domains contained in the C-terminal of the channel has been described. The linkage of these channels to many intracellular metabolites and pathways, as well as their modulation by extracellular natural agents, has been found to be relevant in many physiological processes. This review includes the hallmarks of BK channel biophysics and its physiological impact on specific cells and tissues, highlighting its relationship with auxiliary subunit expression. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-09 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/23668 Contreras, Gustavo F.; Castillo, Karen Noel; Enrique, Nicolás Jorge; Carrasquel Ursulaez, William; Castillo, Juan Pablo; et al.; A BK (Slo1) channel journey from molecule to physiology; Taylor & Francis; Channels; 7; 6; 9-2013; 442-458 1933-6950 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/23668 |
identifier_str_mv |
Contreras, Gustavo F.; Castillo, Karen Noel; Enrique, Nicolás Jorge; Carrasquel Ursulaez, William; Castillo, Juan Pablo; et al.; A BK (Slo1) channel journey from molecule to physiology; Taylor & Francis; Channels; 7; 6; 9-2013; 442-458 1933-6950 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.tandfonline.com/doi/abs/10.4161/chan.26242 info:eu-repo/semantics/altIdentifier/doi/10.4161/chan.26242 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf application/pdf application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Taylor & Francis |
publisher.none.fl_str_mv |
Taylor & Francis |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.070432 |