Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels

Autores
Ozu, Marcelo; Alvear Arias, Juan José; Fernandez, Miguel; Caviglia, Agustín; Peña Pichicoi, Antonio; Carrillo, Christian; Carmona, Emerson; Otero Gonzalez, Anselmo; Garate, José Antonio; Amodeo, Gabriela; Gonzalez, Carlos
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Aquaporins (AQPs) are small transmembrane tetrameric proteins that facilitate water, solute and gas exchange. Their presence has been extensively reported in the biological membranes of almost all living organisms. Although their discovery is much more recent than ion transport systems, different biophysical approaches have contributed to confirm that permeation through each monomer is consistent with closed and open states, introducing the term gating mechanism into the field. The study of AQPs in their native membrane or overexpressed in heterologous systems have experimentally demonstrated that water membrane permeability can be reversibly modified in response to specific modulators. For some regulation mechanisms, such as pH changes, evidence for gating is also supported by high-resolution structures of the water channel in different configurations as well as molecular dynamics simulation. Both experimental and simulation approaches sustain that the rearrangement of conserved residues contributes to occlude the cavity of the channel restricting water permeation. Interestingly, specific charged and conserved residues are present in the environment of the pore and, thus, the tetrameric structure can be subjected to alter the positions of these charges to sustain gating. Thus, is it possible to explore whether the displacement of these charges (gating current) leads to conformational changes? To our knowledge, this question has not yet been addressed at all. In this review, we intend to analyze the suitability of this proposal for the first time.
Fil: Ozu, Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
Fil: Alvear Arias, Juan José. Universidad de Valparaíso; Chile
Fil: Fernandez, Miguel. Universidad de Valparaíso; Chile
Fil: Caviglia, Agustín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
Fil: Peña Pichicoi, Antonio. Universidad de Valparaíso; Chile
Fil: Carrillo, Christian. Universidad de Valparaíso; Chile
Fil: Carmona, Emerson. No especifíca;
Fil: Otero Gonzalez, Anselmo. Universidad de La Habana; Cuba
Fil: Garate, José Antonio. Universidad de Valparaíso; Chile
Fil: Amodeo, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
Fil: Gonzalez, Carlos. Universidad de Valparaíso; Chile
Materia
AQP
AQUAPORIN
GATING MECHANISM
VOLTAGE SENSOR
WATER TRANSPORT
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/212911
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/212911
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Aquaporin Gating: A New Twist to Unravel Permeation through Water ChannelsOzu, MarceloAlvear Arias, Juan JoséFernandez, MiguelCaviglia, AgustínPeña Pichicoi, AntonioCarrillo, ChristianCarmona, EmersonOtero Gonzalez, AnselmoGarate, José AntonioAmodeo, GabrielaGonzalez, CarlosAQPAQUAPORINGATING MECHANISMVOLTAGE SENSORWATER TRANSPORThttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Aquaporins (AQPs) are small transmembrane tetrameric proteins that facilitate water, solute and gas exchange. Their presence has been extensively reported in the biological membranes of almost all living organisms. Although their discovery is much more recent than ion transport systems, different biophysical approaches have contributed to confirm that permeation through each monomer is consistent with closed and open states, introducing the term gating mechanism into the field. The study of AQPs in their native membrane or overexpressed in heterologous systems have experimentally demonstrated that water membrane permeability can be reversibly modified in response to specific modulators. For some regulation mechanisms, such as pH changes, evidence for gating is also supported by high-resolution structures of the water channel in different configurations as well as molecular dynamics simulation. Both experimental and simulation approaches sustain that the rearrangement of conserved residues contributes to occlude the cavity of the channel restricting water permeation. Interestingly, specific charged and conserved residues are present in the environment of the pore and, thus, the tetrameric structure can be subjected to alter the positions of these charges to sustain gating. Thus, is it possible to explore whether the displacement of these charges (gating current) leads to conformational changes? To our knowledge, this question has not yet been addressed at all. In this review, we intend to analyze the suitability of this proposal for the first time.Fil: Ozu, Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; ArgentinaFil: Alvear Arias, Juan José. Universidad de Valparaíso; ChileFil: Fernandez, Miguel. Universidad de Valparaíso; ChileFil: Caviglia, Agustín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; ArgentinaFil: Peña Pichicoi, Antonio. Universidad de Valparaíso; ChileFil: Carrillo, Christian. Universidad de Valparaíso; ChileFil: Carmona, Emerson. No especifíca;Fil: Otero Gonzalez, Anselmo. Universidad de La Habana; CubaFil: Garate, José Antonio. Universidad de Valparaíso; ChileFil: Amodeo, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; ArgentinaFil: Gonzalez, Carlos. Universidad de Valparaíso; ChileMolecular Diversity Preservation International2022-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/212911Ozu, Marcelo; Alvear Arias, Juan José; Fernandez, Miguel; Caviglia, Agustín; Peña Pichicoi, Antonio; et al.; Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 23; 20; 10-2022; 1-291422-0067CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/ijms232012317info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:42:35Zoai:ri.conicet.gov.ar:11336/212911instacron: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 11:42:36.086CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
spellingShingle Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
Ozu, Marcelo
AQP
AQUAPORIN
GATING MECHANISM
VOLTAGE SENSOR
WATER TRANSPORT
title_short Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title_full Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title_fullStr Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title_full_unstemmed Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title_sort Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
dc.creator.none.fl_str_mv Ozu, Marcelo
Alvear Arias, Juan José
Fernandez, Miguel
Caviglia, Agustín
Peña Pichicoi, Antonio
Carrillo, Christian
Carmona, Emerson
Otero Gonzalez, Anselmo
Garate, José Antonio
Amodeo, Gabriela
Gonzalez, Carlos
author Ozu, Marcelo
author_facet Ozu, Marcelo
Alvear Arias, Juan José
Fernandez, Miguel
Caviglia, Agustín
Peña Pichicoi, Antonio
Carrillo, Christian
Carmona, Emerson
Otero Gonzalez, Anselmo
Garate, José Antonio
Amodeo, Gabriela
Gonzalez, Carlos
author_role author
author2 Alvear Arias, Juan José
Fernandez, Miguel
Caviglia, Agustín
Peña Pichicoi, Antonio
Carrillo, Christian
Carmona, Emerson
Otero Gonzalez, Anselmo
Garate, José Antonio
Amodeo, Gabriela
Gonzalez, Carlos
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv AQP
AQUAPORIN
GATING MECHANISM
VOLTAGE SENSOR
WATER TRANSPORT
topic AQP
AQUAPORIN
GATING MECHANISM
VOLTAGE SENSOR
WATER TRANSPORT
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Aquaporins (AQPs) are small transmembrane tetrameric proteins that facilitate water, solute and gas exchange. Their presence has been extensively reported in the biological membranes of almost all living organisms. Although their discovery is much more recent than ion transport systems, different biophysical approaches have contributed to confirm that permeation through each monomer is consistent with closed and open states, introducing the term gating mechanism into the field. The study of AQPs in their native membrane or overexpressed in heterologous systems have experimentally demonstrated that water membrane permeability can be reversibly modified in response to specific modulators. For some regulation mechanisms, such as pH changes, evidence for gating is also supported by high-resolution structures of the water channel in different configurations as well as molecular dynamics simulation. Both experimental and simulation approaches sustain that the rearrangement of conserved residues contributes to occlude the cavity of the channel restricting water permeation. Interestingly, specific charged and conserved residues are present in the environment of the pore and, thus, the tetrameric structure can be subjected to alter the positions of these charges to sustain gating. Thus, is it possible to explore whether the displacement of these charges (gating current) leads to conformational changes? To our knowledge, this question has not yet been addressed at all. In this review, we intend to analyze the suitability of this proposal for the first time.
Fil: Ozu, Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
Fil: Alvear Arias, Juan José. Universidad de Valparaíso; Chile
Fil: Fernandez, Miguel. Universidad de Valparaíso; Chile
Fil: Caviglia, Agustín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
Fil: Peña Pichicoi, Antonio. Universidad de Valparaíso; Chile
Fil: Carrillo, Christian. Universidad de Valparaíso; Chile
Fil: Carmona, Emerson. No especifíca;
Fil: Otero Gonzalez, Anselmo. Universidad de La Habana; Cuba
Fil: Garate, José Antonio. Universidad de Valparaíso; Chile
Fil: Amodeo, Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
Fil: Gonzalez, Carlos. Universidad de Valparaíso; Chile
description Aquaporins (AQPs) are small transmembrane tetrameric proteins that facilitate water, solute and gas exchange. Their presence has been extensively reported in the biological membranes of almost all living organisms. Although their discovery is much more recent than ion transport systems, different biophysical approaches have contributed to confirm that permeation through each monomer is consistent with closed and open states, introducing the term gating mechanism into the field. The study of AQPs in their native membrane or overexpressed in heterologous systems have experimentally demonstrated that water membrane permeability can be reversibly modified in response to specific modulators. For some regulation mechanisms, such as pH changes, evidence for gating is also supported by high-resolution structures of the water channel in different configurations as well as molecular dynamics simulation. Both experimental and simulation approaches sustain that the rearrangement of conserved residues contributes to occlude the cavity of the channel restricting water permeation. Interestingly, specific charged and conserved residues are present in the environment of the pore and, thus, the tetrameric structure can be subjected to alter the positions of these charges to sustain gating. Thus, is it possible to explore whether the displacement of these charges (gating current) leads to conformational changes? To our knowledge, this question has not yet been addressed at all. In this review, we intend to analyze the suitability of this proposal for the first time.
publishDate 2022
dc.date.none.fl_str_mv 2022-10
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/11336/212911
Ozu, Marcelo; Alvear Arias, Juan José; Fernandez, Miguel; Caviglia, Agustín; Peña Pichicoi, Antonio; et al.; Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 23; 20; 10-2022; 1-29
1422-0067
CONICET Digital
CONICET
url http://hdl.handle.net/11336/212911
identifier_str_mv Ozu, Marcelo; Alvear Arias, Juan José; Fernandez, Miguel; Caviglia, Agustín; Peña Pichicoi, Antonio; et al.; Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 23; 20; 10-2022; 1-29
1422-0067
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/ijms232012317
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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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