Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR

Autores
Riedelsberger, Janin; Sharma, Tripti; Gonzalez, Wendy; Gajdanowicz, Pawel; Morales Navarro, Samuel Elías; Garcia-Mata, Carlos; Mueller Roeber, Bernd; González Nilo, Fernando Danilo; Blatt, Michael R.; Dreyer, Ingo
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The family of voltage-gated (Shaker-like) potassium channels in plants includes both inward-rectifying (Kin) channels that allow plant cells to accumulate K+ and outward-rectifying (Kout) channels that mediate K+ efflux. Despite their close structural similarities, Kin and Kout channels differ in their gating sensitivity towards voltage and the extracellular K+ concentration. We have carried out a systematic program of domain swapping between the Kout channel SKOR and the Kin channel KAT1 to examine the impacts on gating of the pore regions, the S4, S5, and the S6 helices. We found that, in particular, the N-terminal part of the S5 played a critical role in KAT1 and SKOR gating. Our findings were supported by molecular dynamics of KAT1 and SKOR homology models. In silico analysis revealed that during channel opening and closing, displacement of certain residues, especially in the S5 and S6 segments, is more pronounced in KAT1 than in SKOR. From our analysis of the S4–S6 region, we conclude that gating (and K+-sensing in SKOR) depend on a number of structural elements that are dispersed over this ∼145-residue sequence and that these place additional constraints on configurational rearrangement of the channels during gating.
Fil: Riedelsberger, Janin . Universität Potsdam; Alemania. Max-Planck Institute of Molecular Plant Physiology; Alemania
Fil: Sharma, Tripti . Universität Potsdam; Alemania. Max-Planck Institute of Molecular Plant Physiology; Alemania
Fil: Gonzalez, Wendy . Universidad de Talca; Chile
Fil: Gajdanowicz, Pawel . Universität Potsdam; Alemania
Fil: Morales Navarro, Samuel Elías . Universidad de Talca; Chile
Fil: Garcia-Mata, Carlos. University Of Glasgow; Reino Unido. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Mueller Roeber, Bernd. Max-Planck Institute of Molecular Plant Physiology; Alemania. Universität Potsdam; Alemania
Fil: González Nilo, Fernando Danilo . Universidad de Talca; Chile
Fil: Blatt, Michael R. . University Of Glasgow; Reino Unido
Fil: Dreyer, Ingo . Universität Potsdam; Alemania
Materia
Arabidopsis
K+ Channel
Outward Rectifier
Inward Rectifier
Channel Protein Structure
Channel Protein–Cation Interaction
Gating
K+-Dependent
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/13211
Acceder
id CONICETDig_93015e262e02459ce1625b889bd4bde4
oai_identifier_str oai:ri.conicet.gov.ar:11336/13211
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKORRiedelsberger, Janin Sharma, Tripti Gonzalez, Wendy Gajdanowicz, Pawel Morales Navarro, Samuel Elías Garcia-Mata, CarlosMueller Roeber, BerndGonzález Nilo, Fernando Danilo Blatt, Michael R. Dreyer, Ingo ArabidopsisK+ ChannelOutward RectifierInward RectifierChannel Protein StructureChannel Protein–Cation InteractionGatingK+-Dependenthttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The family of voltage-gated (Shaker-like) potassium channels in plants includes both inward-rectifying (Kin) channels that allow plant cells to accumulate K+ and outward-rectifying (Kout) channels that mediate K+ efflux. Despite their close structural similarities, Kin and Kout channels differ in their gating sensitivity towards voltage and the extracellular K+ concentration. We have carried out a systematic program of domain swapping between the Kout channel SKOR and the Kin channel KAT1 to examine the impacts on gating of the pore regions, the S4, S5, and the S6 helices. We found that, in particular, the N-terminal part of the S5 played a critical role in KAT1 and SKOR gating. Our findings were supported by molecular dynamics of KAT1 and SKOR homology models. In silico analysis revealed that during channel opening and closing, displacement of certain residues, especially in the S5 and S6 segments, is more pronounced in KAT1 than in SKOR. From our analysis of the S4–S6 region, we conclude that gating (and K+-sensing in SKOR) depend on a number of structural elements that are dispersed over this ∼145-residue sequence and that these place additional constraints on configurational rearrangement of the channels during gating.Fil: Riedelsberger, Janin . Universität Potsdam; Alemania. Max-Planck Institute of Molecular Plant Physiology; AlemaniaFil: Sharma, Tripti . Universität Potsdam; Alemania. Max-Planck Institute of Molecular Plant Physiology; AlemaniaFil: Gonzalez, Wendy . Universidad de Talca; ChileFil: Gajdanowicz, Pawel . Universität Potsdam; AlemaniaFil: Morales Navarro, Samuel Elías . Universidad de Talca; ChileFil: Garcia-Mata, Carlos. University Of Glasgow; Reino Unido. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Mueller Roeber, Bernd. Max-Planck Institute of Molecular Plant Physiology; Alemania. Universität Potsdam; AlemaniaFil: González Nilo, Fernando Danilo . Universidad de Talca; ChileFil: Blatt, Michael R. . University Of Glasgow; Reino UnidoFil: Dreyer, Ingo . Universität Potsdam; AlemaniaElsevier2010-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/13211Riedelsberger, Janin ; Sharma, Tripti ; Gonzalez, Wendy ; Gajdanowicz, Pawel ; Morales Navarro, Samuel Elías ; et al.; Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR; Elsevier; Molecular Plant; 3; 1; 1-2010; 236-2451674-2052enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1674205214604093info:eu-repo/semantics/altIdentifier/doi/10.1093/mp/ssp096info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:42:58Zoai:ri.conicet.gov.ar:11336/13211instacron: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 09:42:59.039CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR
title Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR
spellingShingle Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR
Riedelsberger, Janin
Arabidopsis
K+ Channel
Outward Rectifier
Inward Rectifier
Channel Protein Structure
Channel Protein–Cation Interaction
Gating
K+-Dependent
title_short Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR
title_full Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR
title_fullStr Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR
title_full_unstemmed Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR
title_sort Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR
dc.creator.none.fl_str_mv Riedelsberger, Janin
Sharma, Tripti
Gonzalez, Wendy
Gajdanowicz, Pawel
Morales Navarro, Samuel Elías
Garcia-Mata, Carlos
Mueller Roeber, Bernd
González Nilo, Fernando Danilo
Blatt, Michael R.
Dreyer, Ingo
author Riedelsberger, Janin
author_facet Riedelsberger, Janin
Sharma, Tripti
Gonzalez, Wendy
Gajdanowicz, Pawel
Morales Navarro, Samuel Elías
Garcia-Mata, Carlos
Mueller Roeber, Bernd
González Nilo, Fernando Danilo
Blatt, Michael R.
Dreyer, Ingo
author_role author
author2 Sharma, Tripti
Gonzalez, Wendy
Gajdanowicz, Pawel
Morales Navarro, Samuel Elías
Garcia-Mata, Carlos
Mueller Roeber, Bernd
González Nilo, Fernando Danilo
Blatt, Michael R.
Dreyer, Ingo
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Arabidopsis
K+ Channel
Outward Rectifier
Inward Rectifier
Channel Protein Structure
Channel Protein–Cation Interaction
Gating
K+-Dependent
topic Arabidopsis
K+ Channel
Outward Rectifier
Inward Rectifier
Channel Protein Structure
Channel Protein–Cation Interaction
Gating
K+-Dependent
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The family of voltage-gated (Shaker-like) potassium channels in plants includes both inward-rectifying (Kin) channels that allow plant cells to accumulate K+ and outward-rectifying (Kout) channels that mediate K+ efflux. Despite their close structural similarities, Kin and Kout channels differ in their gating sensitivity towards voltage and the extracellular K+ concentration. We have carried out a systematic program of domain swapping between the Kout channel SKOR and the Kin channel KAT1 to examine the impacts on gating of the pore regions, the S4, S5, and the S6 helices. We found that, in particular, the N-terminal part of the S5 played a critical role in KAT1 and SKOR gating. Our findings were supported by molecular dynamics of KAT1 and SKOR homology models. In silico analysis revealed that during channel opening and closing, displacement of certain residues, especially in the S5 and S6 segments, is more pronounced in KAT1 than in SKOR. From our analysis of the S4–S6 region, we conclude that gating (and K+-sensing in SKOR) depend on a number of structural elements that are dispersed over this ∼145-residue sequence and that these place additional constraints on configurational rearrangement of the channels during gating.
Fil: Riedelsberger, Janin . Universität Potsdam; Alemania. Max-Planck Institute of Molecular Plant Physiology; Alemania
Fil: Sharma, Tripti . Universität Potsdam; Alemania. Max-Planck Institute of Molecular Plant Physiology; Alemania
Fil: Gonzalez, Wendy . Universidad de Talca; Chile
Fil: Gajdanowicz, Pawel . Universität Potsdam; Alemania
Fil: Morales Navarro, Samuel Elías . Universidad de Talca; Chile
Fil: Garcia-Mata, Carlos. University Of Glasgow; Reino Unido. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Mueller Roeber, Bernd. Max-Planck Institute of Molecular Plant Physiology; Alemania. Universität Potsdam; Alemania
Fil: González Nilo, Fernando Danilo . Universidad de Talca; Chile
Fil: Blatt, Michael R. . University Of Glasgow; Reino Unido
Fil: Dreyer, Ingo . Universität Potsdam; Alemania
description The family of voltage-gated (Shaker-like) potassium channels in plants includes both inward-rectifying (Kin) channels that allow plant cells to accumulate K+ and outward-rectifying (Kout) channels that mediate K+ efflux. Despite their close structural similarities, Kin and Kout channels differ in their gating sensitivity towards voltage and the extracellular K+ concentration. We have carried out a systematic program of domain swapping between the Kout channel SKOR and the Kin channel KAT1 to examine the impacts on gating of the pore regions, the S4, S5, and the S6 helices. We found that, in particular, the N-terminal part of the S5 played a critical role in KAT1 and SKOR gating. Our findings were supported by molecular dynamics of KAT1 and SKOR homology models. In silico analysis revealed that during channel opening and closing, displacement of certain residues, especially in the S5 and S6 segments, is more pronounced in KAT1 than in SKOR. From our analysis of the S4–S6 region, we conclude that gating (and K+-sensing in SKOR) depend on a number of structural elements that are dispersed over this ∼145-residue sequence and that these place additional constraints on configurational rearrangement of the channels during gating.
publishDate 2010
dc.date.none.fl_str_mv 2010-01
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/11336/13211
Riedelsberger, Janin ; Sharma, Tripti ; Gonzalez, Wendy ; Gajdanowicz, Pawel ; Morales Navarro, Samuel Elías ; et al.; Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR; Elsevier; Molecular Plant; 3; 1; 1-2010; 236-245
1674-2052
url http://hdl.handle.net/11336/13211
identifier_str_mv Riedelsberger, Janin ; Sharma, Tripti ; Gonzalez, Wendy ; Gajdanowicz, Pawel ; Morales Navarro, Samuel Elías ; et al.; Distributed structures underlie gating differences between the K in Channel KAT1 and the K out Channel SKOR; Elsevier; Molecular Plant; 3; 1; 1-2010; 236-245
1674-2052
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1674205214604093
info:eu-repo/semantics/altIdentifier/doi/10.1093/mp/ssp096
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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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score 13.070432

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