Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity
- Autores
- Gajdanowicz, Pawel; Garcia-Mata, Carlos; Gonzalez, Wendy; Morales Navarro, Samuel Elías; Sharma, Tripti; Gonzalez Nilo, Fernando Danilo; Gutowicz, Jan; Mueller Roeber, Bernd; Blatt, Michael R.; Dreyer, Ingo
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- • The family of voltage-gated potassium channels in plants presumably evolved from a common ancestor and 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, the activity of Kin channels is largely independent of K+ and depends only on the transmembrane voltage, whereas that of Kout channels responds to the membrane voltage and the prevailing extracellular K+ concentration. Gating of potassium channels is achieved by structural rearrangements within the last transmembrane domain (S6). • Here we investigated the functional equivalence of the S6 helices of the Kin channel KAT1 and the Kout channel SKOR by domain-swapping and site-directed mutagenesis. Channel mutants and chimeras were analyzed after expression in Xenopus oocytes. • We identified two discrete regions that influence gating differently in both channels, demonstrating a lack of functional complementarity between KAT1 and SKOR. Our findings are supported by molecular models of KAT1 and SKOR in the open and closed states. • The role of the S6 segment in gating evolved differently during specialization of the two channel subclasses, posing an obstacle for the transfer of the K+-sensor from Kout to Kin channels.
Fil: Gajdanowicz, Pawel. Universität Potsdam; Alemania
Fil: Garcia-Mata, Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas. Laboratorio de Fisiología Molecular e Integrativa; Argentina. University of Glasgow; Reino Unido
Fil: Gonzalez, Wendy. Universidad de Talca; Chile. Universität Potsdam; Alemania
Fil: Morales Navarro, Samuel Elías. Universidad de Talca; Chile
Fil: Sharma, Tripti. Max Planck Institute of Molecular Plant Physiology; Alemania. Universität Potsdam; Alemania
Fil: Gonzalez Nilo, Fernando Danilo. Universidad de Talca; Chile
Fil: Gutowicz, Jan. University of Wroclaw; Polonia
Fil: Mueller Roeber, Bernd. Max Planck Institute of Molecular Plant Physiology; Alemania. Universität Potsdam; Alemania
Fil: Blatt, Michael R.. University of Glasgow; Reino Unido
Fil: Dreyer, Ingo. Universität Potsdam; Alemania - Materia
-
CHANNEL PROTEIN STRUCTURE
CHANNEL PROTEIN-CATION INTERACTION
INWARD RECTIFYING K CHANNEL
OUTWARD RECTIFYING K CHANNEL - 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:11336/105126
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/105126 |
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network_name_str |
CONICET Digital (CONICET) |
spelling |
Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activityGajdanowicz, PawelGarcia-Mata, CarlosGonzalez, WendyMorales Navarro, Samuel ElíasSharma, TriptiGonzalez Nilo, Fernando DaniloGutowicz, JanMueller Roeber, BerndBlatt, Michael R.Dreyer, IngoCHANNEL PROTEIN STRUCTURECHANNEL PROTEIN-CATION INTERACTIONINWARD RECTIFYING K CHANNELOUTWARD RECTIFYING K CHANNELhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1• The family of voltage-gated potassium channels in plants presumably evolved from a common ancestor and 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, the activity of Kin channels is largely independent of K+ and depends only on the transmembrane voltage, whereas that of Kout channels responds to the membrane voltage and the prevailing extracellular K+ concentration. Gating of potassium channels is achieved by structural rearrangements within the last transmembrane domain (S6). • Here we investigated the functional equivalence of the S6 helices of the Kin channel KAT1 and the Kout channel SKOR by domain-swapping and site-directed mutagenesis. Channel mutants and chimeras were analyzed after expression in Xenopus oocytes. • We identified two discrete regions that influence gating differently in both channels, demonstrating a lack of functional complementarity between KAT1 and SKOR. Our findings are supported by molecular models of KAT1 and SKOR in the open and closed states. • The role of the S6 segment in gating evolved differently during specialization of the two channel subclasses, posing an obstacle for the transfer of the K+-sensor from Kout to Kin channels.Fil: Gajdanowicz, Pawel. Universität Potsdam; AlemaniaFil: Garcia-Mata, Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas. Laboratorio de Fisiología Molecular e Integrativa; Argentina. University of Glasgow; Reino UnidoFil: Gonzalez, Wendy. Universidad de Talca; Chile. Universität Potsdam; AlemaniaFil: Morales Navarro, Samuel Elías. Universidad de Talca; ChileFil: Sharma, Tripti. Max Planck Institute of Molecular Plant Physiology; Alemania. Universität Potsdam; AlemaniaFil: Gonzalez Nilo, Fernando Danilo. Universidad de Talca; ChileFil: Gutowicz, Jan. University of Wroclaw; PoloniaFil: Mueller Roeber, Bernd. Max Planck Institute of Molecular Plant Physiology; Alemania. Universität Potsdam; AlemaniaFil: Blatt, Michael R.. University of Glasgow; Reino UnidoFil: Dreyer, Ingo. Universität Potsdam; AlemaniaWiley Blackwell Publishing, Inc2009-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/105126Gajdanowicz, Pawel; Garcia-Mata, Carlos; Gonzalez, Wendy; Morales Navarro, Samuel Elías; Sharma, Tripti; et al.; Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity; Wiley Blackwell Publishing, Inc; New Phytologist; 182; 2; 4-2009; 380-3910028-646XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1469-8137.2008.02749.xinfo:eu-repo/semantics/altIdentifier/url/https://nph.onlinelibrary.wiley.com/doi/full/10.1111/j.1469-8137.2008.02749.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:46:43Zoai:ri.conicet.gov.ar:11336/105126instacron: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 10:46:43.769CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity |
title |
Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity |
spellingShingle |
Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity Gajdanowicz, Pawel CHANNEL PROTEIN STRUCTURE CHANNEL PROTEIN-CATION INTERACTION INWARD RECTIFYING K CHANNEL OUTWARD RECTIFYING K CHANNEL |
title_short |
Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity |
title_full |
Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity |
title_fullStr |
Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity |
title_full_unstemmed |
Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity |
title_sort |
Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity |
dc.creator.none.fl_str_mv |
Gajdanowicz, Pawel Garcia-Mata, Carlos Gonzalez, Wendy Morales Navarro, Samuel Elías Sharma, Tripti Gonzalez Nilo, Fernando Danilo Gutowicz, Jan Mueller Roeber, Bernd Blatt, Michael R. Dreyer, Ingo |
author |
Gajdanowicz, Pawel |
author_facet |
Gajdanowicz, Pawel Garcia-Mata, Carlos Gonzalez, Wendy Morales Navarro, Samuel Elías Sharma, Tripti Gonzalez Nilo, Fernando Danilo Gutowicz, Jan Mueller Roeber, Bernd Blatt, Michael R. Dreyer, Ingo |
author_role |
author |
author2 |
Garcia-Mata, Carlos Gonzalez, Wendy Morales Navarro, Samuel Elías Sharma, Tripti Gonzalez Nilo, Fernando Danilo Gutowicz, Jan Mueller Roeber, Bernd Blatt, Michael R. Dreyer, Ingo |
author2_role |
author author author author author author author author author |
dc.subject.none.fl_str_mv |
CHANNEL PROTEIN STRUCTURE CHANNEL PROTEIN-CATION INTERACTION INWARD RECTIFYING K CHANNEL OUTWARD RECTIFYING K CHANNEL |
topic |
CHANNEL PROTEIN STRUCTURE CHANNEL PROTEIN-CATION INTERACTION INWARD RECTIFYING K CHANNEL OUTWARD RECTIFYING K CHANNEL |
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 potassium channels in plants presumably evolved from a common ancestor and 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, the activity of Kin channels is largely independent of K+ and depends only on the transmembrane voltage, whereas that of Kout channels responds to the membrane voltage and the prevailing extracellular K+ concentration. Gating of potassium channels is achieved by structural rearrangements within the last transmembrane domain (S6). • Here we investigated the functional equivalence of the S6 helices of the Kin channel KAT1 and the Kout channel SKOR by domain-swapping and site-directed mutagenesis. Channel mutants and chimeras were analyzed after expression in Xenopus oocytes. • We identified two discrete regions that influence gating differently in both channels, demonstrating a lack of functional complementarity between KAT1 and SKOR. Our findings are supported by molecular models of KAT1 and SKOR in the open and closed states. • The role of the S6 segment in gating evolved differently during specialization of the two channel subclasses, posing an obstacle for the transfer of the K+-sensor from Kout to Kin channels. Fil: Gajdanowicz, Pawel. Universität Potsdam; Alemania Fil: Garcia-Mata, Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas. Laboratorio de Fisiología Molecular e Integrativa; Argentina. University of Glasgow; Reino Unido Fil: Gonzalez, Wendy. Universidad de Talca; Chile. Universität Potsdam; Alemania Fil: Morales Navarro, Samuel Elías. Universidad de Talca; Chile Fil: Sharma, Tripti. Max Planck Institute of Molecular Plant Physiology; Alemania. Universität Potsdam; Alemania Fil: Gonzalez Nilo, Fernando Danilo. Universidad de Talca; Chile Fil: Gutowicz, Jan. University of Wroclaw; Polonia Fil: Mueller Roeber, Bernd. Max Planck Institute of Molecular Plant Physiology; Alemania. Universität Potsdam; Alemania Fil: Blatt, Michael R.. University of Glasgow; Reino Unido Fil: Dreyer, Ingo. Universität Potsdam; Alemania |
description |
• The family of voltage-gated potassium channels in plants presumably evolved from a common ancestor and 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, the activity of Kin channels is largely independent of K+ and depends only on the transmembrane voltage, whereas that of Kout channels responds to the membrane voltage and the prevailing extracellular K+ concentration. Gating of potassium channels is achieved by structural rearrangements within the last transmembrane domain (S6). • Here we investigated the functional equivalence of the S6 helices of the Kin channel KAT1 and the Kout channel SKOR by domain-swapping and site-directed mutagenesis. Channel mutants and chimeras were analyzed after expression in Xenopus oocytes. • We identified two discrete regions that influence gating differently in both channels, demonstrating a lack of functional complementarity between KAT1 and SKOR. Our findings are supported by molecular models of KAT1 and SKOR in the open and closed states. • The role of the S6 segment in gating evolved differently during specialization of the two channel subclasses, posing an obstacle for the transfer of the K+-sensor from Kout to Kin channels. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-04 |
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/11336/105126 Gajdanowicz, Pawel; Garcia-Mata, Carlos; Gonzalez, Wendy; Morales Navarro, Samuel Elías; Sharma, Tripti; et al.; Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity; Wiley Blackwell Publishing, Inc; New Phytologist; 182; 2; 4-2009; 380-391 0028-646X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/105126 |
identifier_str_mv |
Gajdanowicz, Pawel; Garcia-Mata, Carlos; Gonzalez, Wendy; Morales Navarro, Samuel Elías; Sharma, Tripti; et al.; Distinct roles of the last transmembrane domain in controlling Arabidopsis K + channel activity; Wiley Blackwell Publishing, Inc; New Phytologist; 182; 2; 4-2009; 380-391 0028-646X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1469-8137.2008.02749.x info:eu-repo/semantics/altIdentifier/url/https://nph.onlinelibrary.wiley.com/doi/full/10.1111/j.1469-8137.2008.02749.x |
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 |
dc.publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
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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1844614509454426112 |
score |
13.070432 |