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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/105126
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/105126
network_acronym_str CONICETDig
repository_id_str 3498
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 Técnicas2025-10-22T12:20:07Zoai: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:34982025-10-22 12:20:07.337CONICET 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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score 12.982451

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