Aquaporins: More than functional monomers in a tetrameric arrangement

Autores
Ozu, Marcelo; Galizia, Luciano; Acuña, Cynthia Florencia; Amodeo, Gabriela
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Aquaporins (AQPs) function as tetrameric structures in which each monomer has its ownpermeable pathway. The combination of structural biology, molecular dynamics simulations, andexperimental approaches has contributed to improve our knowledge of how protein conformationalchanges can challenge its transport capacity, rapidly altering the membrane permeability. This reviewis focused on evidence that highlights the functional relationship between the monomers and thetetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanismsthat affect the monomer, the tetramer, or tetramers combined in complex structures. We thereforeexplore: (i) water permeation and recent evidence on ion permeation, including the permeation pathwaycontroversy?each monomer versus the central pore of the tetramer?and (ii) regulatory mechanismsthat cannot be attributed to independent monomers. In particular, we discuss channel gating andAQPs that sense membrane tension. For the latter we propose a possible mechanism that includes themonomer (slight changes of pore shape, the number of possible H-bonds between water molecules andpore-lining residues) and the tetramer (interactions among monomers and a positive cooperative effect).
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: Galizia, Luciano. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; Argentina
Fil: Acuña, Cynthia Florencia. 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: 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
Materia
acuaporinas
permeabilididad osmotica
canales de agua
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:11336/86865
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Aquaporins: More than functional monomers in a tetrameric arrangementOzu, MarceloGalizia, LucianoAcuña, Cynthia FlorenciaAmodeo, Gabrielaacuaporinaspermeabilididad osmoticacanales de aguahttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Aquaporins (AQPs) function as tetrameric structures in which each monomer has its ownpermeable pathway. The combination of structural biology, molecular dynamics simulations, andexperimental approaches has contributed to improve our knowledge of how protein conformationalchanges can challenge its transport capacity, rapidly altering the membrane permeability. This reviewis focused on evidence that highlights the functional relationship between the monomers and thetetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanismsthat affect the monomer, the tetramer, or tetramers combined in complex structures. We thereforeexplore: (i) water permeation and recent evidence on ion permeation, including the permeation pathwaycontroversy?each monomer versus the central pore of the tetramer?and (ii) regulatory mechanismsthat cannot be attributed to independent monomers. In particular, we discuss channel gating andAQPs that sense membrane tension. For the latter we propose a possible mechanism that includes themonomer (slight changes of pore shape, the number of possible H-bonds between water molecules andpore-lining residues) and the tetramer (interactions among monomers and a positive cooperative effect).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: Galizia, Luciano. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; ArgentinaFil: Acuña, Cynthia Florencia. 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: 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; ArgentinaMDPI2018-11info: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/11336/86865Ozu, Marcelo; Galizia, Luciano; Acuña, Cynthia Florencia; Amodeo, Gabriela; Aquaporins: More than functional monomers in a tetrameric arrangement; MDPI; Cells; 7; 11; 11-2018; 1-242073-4409CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/2073-4409/7/11/209info:eu-repo/semantics/altIdentifier/doi/10.3390/cells7110209info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:51:29Zoai:ri.conicet.gov.ar:11336/86865instacron: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 09:51:30.258CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aquaporins: More than functional monomers in a tetrameric arrangement
title Aquaporins: More than functional monomers in a tetrameric arrangement
spellingShingle Aquaporins: More than functional monomers in a tetrameric arrangement
Ozu, Marcelo
acuaporinas
permeabilididad osmotica
canales de agua
title_short Aquaporins: More than functional monomers in a tetrameric arrangement
title_full Aquaporins: More than functional monomers in a tetrameric arrangement
title_fullStr Aquaporins: More than functional monomers in a tetrameric arrangement
title_full_unstemmed Aquaporins: More than functional monomers in a tetrameric arrangement
title_sort Aquaporins: More than functional monomers in a tetrameric arrangement
dc.creator.none.fl_str_mv Ozu, Marcelo
Galizia, Luciano
Acuña, Cynthia Florencia
Amodeo, Gabriela
author Ozu, Marcelo
author_facet Ozu, Marcelo
Galizia, Luciano
Acuña, Cynthia Florencia
Amodeo, Gabriela
author_role author
author2 Galizia, Luciano
Acuña, Cynthia Florencia
Amodeo, Gabriela
author2_role author
author
author
dc.subject.none.fl_str_mv acuaporinas
permeabilididad osmotica
canales de agua
topic acuaporinas
permeabilididad osmotica
canales de agua
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) function as tetrameric structures in which each monomer has its ownpermeable pathway. The combination of structural biology, molecular dynamics simulations, andexperimental approaches has contributed to improve our knowledge of how protein conformationalchanges can challenge its transport capacity, rapidly altering the membrane permeability. This reviewis focused on evidence that highlights the functional relationship between the monomers and thetetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanismsthat affect the monomer, the tetramer, or tetramers combined in complex structures. We thereforeexplore: (i) water permeation and recent evidence on ion permeation, including the permeation pathwaycontroversy?each monomer versus the central pore of the tetramer?and (ii) regulatory mechanismsthat cannot be attributed to independent monomers. In particular, we discuss channel gating andAQPs that sense membrane tension. For the latter we propose a possible mechanism that includes themonomer (slight changes of pore shape, the number of possible H-bonds between water molecules andpore-lining residues) and the tetramer (interactions among monomers and a positive cooperative effect).
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: Galizia, Luciano. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Médicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Médicas; Argentina
Fil: Acuña, Cynthia Florencia. 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: 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
description Aquaporins (AQPs) function as tetrameric structures in which each monomer has its ownpermeable pathway. The combination of structural biology, molecular dynamics simulations, andexperimental approaches has contributed to improve our knowledge of how protein conformationalchanges can challenge its transport capacity, rapidly altering the membrane permeability. This reviewis focused on evidence that highlights the functional relationship between the monomers and thetetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanismsthat affect the monomer, the tetramer, or tetramers combined in complex structures. We thereforeexplore: (i) water permeation and recent evidence on ion permeation, including the permeation pathwaycontroversy?each monomer versus the central pore of the tetramer?and (ii) regulatory mechanismsthat cannot be attributed to independent monomers. In particular, we discuss channel gating andAQPs that sense membrane tension. For the latter we propose a possible mechanism that includes themonomer (slight changes of pore shape, the number of possible H-bonds between water molecules andpore-lining residues) and the tetramer (interactions among monomers and a positive cooperative effect).
publishDate 2018
dc.date.none.fl_str_mv 2018-11
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/11336/86865
Ozu, Marcelo; Galizia, Luciano; Acuña, Cynthia Florencia; Amodeo, Gabriela; Aquaporins: More than functional monomers in a tetrameric arrangement; MDPI; Cells; 7; 11; 11-2018; 1-24
2073-4409
CONICET Digital
CONICET
url http://hdl.handle.net/11336/86865
identifier_str_mv Ozu, Marcelo; Galizia, Luciano; Acuña, Cynthia Florencia; Amodeo, Gabriela; Aquaporins: More than functional monomers in a tetrameric arrangement; MDPI; Cells; 7; 11; 11-2018; 1-24
2073-4409
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.mdpi.com/2073-4409/7/11/209
info:eu-repo/semantics/altIdentifier/doi/10.3390/cells7110209
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
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
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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