Cooperativity in proton sensing by PIP aquaporins

Autores
Vitali, Victoria Andrea; Jozefkowicz, Cintia; Canessa Fortuna, Agustina; Soto, Gabriela Cinthia; Gonzalez Flecha, Francisco Luis; Alleva, Karina Edith
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
One of the most intriguing properties of plasma membrane intrinsic protein (PIP) aquaporins (AQPs) is their ability to modulate water transport by sensing different levels of intracellular pH through the assembly of homo‐ and heterotetrameric molecular species in the plasma membrane. In this work, using a phenomenological modeling approach, we demonstrate that cooperativity in PIP biological response cannot be directly attributed to a cooperative proton binding, as it is usually considered, since it could also be the consequence of a cooperative conformation transition between open and closed states of the channel. Moreover, our results show that, when mixed populations of homo‐ and heterotetrameric PIP channels are coexpressed in the plasma membrane of the same cell, the observed decrease in the degree of positive cooperativity would result from the simultaneous presence of molecular species with different levels of proton sensing. Indeed, the random mixing between different PIP paralogues as subunits in a single tetramer, plus the possibility of mixed populations of homo‐ and heterotetrameric PIP channels widen the spectrum of cooperative responses of a cell membrane. Our approach offers a deep understanding of cooperative transport of AQP channels, as members of a multiprotein family where the relevant proton binding sites of each member have not been clearly elucidated yet.
Instituto de Genética
Fil: Vitali, Victoria Andrea. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; Argentina
Fil: Jozefkowicz, Cintia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Canessa Fortuna, Agustina. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; Argentina
Fil: Soto, Gabriela Cinthia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gonzalez Flecha, Francisco Luis. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina.
Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; Argentina
Fuente
The Febs journal 286 (5) : 991-1002 (Marzo 2019)
Materia
Plant Water Relations
Cell Membranes
Relaciones Planta Agua
Membranas Celulares
Aquaporin
Acuaporinas
Nivel de accesibilidad
acceso restringido
Condiciones de uso
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/5031
Acceder
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oai_identifier_str oai:localhost:20.500.12123/5031
network_acronym_str INTADig
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network_name_str INTA Digital (INTA)
spelling Cooperativity in proton sensing by PIP aquaporinsVitali, Victoria AndreaJozefkowicz, CintiaCanessa Fortuna, AgustinaSoto, Gabriela CinthiaGonzalez Flecha, Francisco LuisAlleva, Karina EdithPlant Water RelationsCell MembranesRelaciones Planta AguaMembranas CelularesAquaporinAcuaporinasOne of the most intriguing properties of plasma membrane intrinsic protein (PIP) aquaporins (AQPs) is their ability to modulate water transport by sensing different levels of intracellular pH through the assembly of homo‐ and heterotetrameric molecular species in the plasma membrane. In this work, using a phenomenological modeling approach, we demonstrate that cooperativity in PIP biological response cannot be directly attributed to a cooperative proton binding, as it is usually considered, since it could also be the consequence of a cooperative conformation transition between open and closed states of the channel. Moreover, our results show that, when mixed populations of homo‐ and heterotetrameric PIP channels are coexpressed in the plasma membrane of the same cell, the observed decrease in the degree of positive cooperativity would result from the simultaneous presence of molecular species with different levels of proton sensing. Indeed, the random mixing between different PIP paralogues as subunits in a single tetramer, plus the possibility of mixed populations of homo‐ and heterotetrameric PIP channels widen the spectrum of cooperative responses of a cell membrane. Our approach offers a deep understanding of cooperative transport of AQP channels, as members of a multiprotein family where the relevant proton binding sites of each member have not been clearly elucidated yet.Instituto de GenéticaFil: Vitali, Victoria Andrea. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; ArgentinaFil: Jozefkowicz, Cintia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Canessa Fortuna, Agustina. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; ArgentinaFil: Soto, Gabriela Cinthia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Gonzalez Flecha, Francisco Luis. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina.Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; ArgentinaWiley2019-05-03T16:42:26Z2019-05-03T16:42:26Z2019-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.14701http://hdl.handle.net/20.500.12123/50311742-464Xhttps://doi.org/10.1111/febs.14701The Febs journal 286 (5) : 991-1002 (Marzo 2019)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/restrictedAccess2025-09-29T13:44:38Zoai:localhost:20.500.12123/5031instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-29 13:44:39.248INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Cooperativity in proton sensing by PIP aquaporins
title Cooperativity in proton sensing by PIP aquaporins
spellingShingle Cooperativity in proton sensing by PIP aquaporins
Vitali, Victoria Andrea
Plant Water Relations
Cell Membranes
Relaciones Planta Agua
Membranas Celulares
Aquaporin
Acuaporinas
title_short Cooperativity in proton sensing by PIP aquaporins
title_full Cooperativity in proton sensing by PIP aquaporins
title_fullStr Cooperativity in proton sensing by PIP aquaporins
title_full_unstemmed Cooperativity in proton sensing by PIP aquaporins
title_sort Cooperativity in proton sensing by PIP aquaporins
dc.creator.none.fl_str_mv Vitali, Victoria Andrea
Jozefkowicz, Cintia
Canessa Fortuna, Agustina
Soto, Gabriela Cinthia
Gonzalez Flecha, Francisco Luis
Alleva, Karina Edith
author Vitali, Victoria Andrea
author_facet Vitali, Victoria Andrea
Jozefkowicz, Cintia
Canessa Fortuna, Agustina
Soto, Gabriela Cinthia
Gonzalez Flecha, Francisco Luis
Alleva, Karina Edith
author_role author
author2 Jozefkowicz, Cintia
Canessa Fortuna, Agustina
Soto, Gabriela Cinthia
Gonzalez Flecha, Francisco Luis
Alleva, Karina Edith
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Plant Water Relations
Cell Membranes
Relaciones Planta Agua
Membranas Celulares
Aquaporin
Acuaporinas
topic Plant Water Relations
Cell Membranes
Relaciones Planta Agua
Membranas Celulares
Aquaporin
Acuaporinas
dc.description.none.fl_txt_mv One of the most intriguing properties of plasma membrane intrinsic protein (PIP) aquaporins (AQPs) is their ability to modulate water transport by sensing different levels of intracellular pH through the assembly of homo‐ and heterotetrameric molecular species in the plasma membrane. In this work, using a phenomenological modeling approach, we demonstrate that cooperativity in PIP biological response cannot be directly attributed to a cooperative proton binding, as it is usually considered, since it could also be the consequence of a cooperative conformation transition between open and closed states of the channel. Moreover, our results show that, when mixed populations of homo‐ and heterotetrameric PIP channels are coexpressed in the plasma membrane of the same cell, the observed decrease in the degree of positive cooperativity would result from the simultaneous presence of molecular species with different levels of proton sensing. Indeed, the random mixing between different PIP paralogues as subunits in a single tetramer, plus the possibility of mixed populations of homo‐ and heterotetrameric PIP channels widen the spectrum of cooperative responses of a cell membrane. Our approach offers a deep understanding of cooperative transport of AQP channels, as members of a multiprotein family where the relevant proton binding sites of each member have not been clearly elucidated yet.
Instituto de Genética
Fil: Vitali, Victoria Andrea. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; Argentina
Fil: Jozefkowicz, Cintia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Canessa Fortuna, Agustina. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; Argentina
Fil: Soto, Gabriela Cinthia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gonzalez Flecha, Francisco Luis. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina.
Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Cientificas y Tecnicas; Ciudad Universitaria. Instituto de Química y Fisicoquímica Biológica. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Fisicoquímica Biológica; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; Argentina
description One of the most intriguing properties of plasma membrane intrinsic protein (PIP) aquaporins (AQPs) is their ability to modulate water transport by sensing different levels of intracellular pH through the assembly of homo‐ and heterotetrameric molecular species in the plasma membrane. In this work, using a phenomenological modeling approach, we demonstrate that cooperativity in PIP biological response cannot be directly attributed to a cooperative proton binding, as it is usually considered, since it could also be the consequence of a cooperative conformation transition between open and closed states of the channel. Moreover, our results show that, when mixed populations of homo‐ and heterotetrameric PIP channels are coexpressed in the plasma membrane of the same cell, the observed decrease in the degree of positive cooperativity would result from the simultaneous presence of molecular species with different levels of proton sensing. Indeed, the random mixing between different PIP paralogues as subunits in a single tetramer, plus the possibility of mixed populations of homo‐ and heterotetrameric PIP channels widen the spectrum of cooperative responses of a cell membrane. Our approach offers a deep understanding of cooperative transport of AQP channels, as members of a multiprotein family where the relevant proton binding sites of each member have not been clearly elucidated yet.
publishDate 2019
dc.date.none.fl_str_mv 2019-05-03T16:42:26Z
2019-05-03T16:42:26Z
2019-03
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 https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.14701
http://hdl.handle.net/20.500.12123/5031
1742-464X
https://doi.org/10.1111/febs.14701
url https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.14701
http://hdl.handle.net/20.500.12123/5031
https://doi.org/10.1111/febs.14701
identifier_str_mv 1742-464X
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/restrictedAccess
eu_rights_str_mv restrictedAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv The Febs journal 286 (5) : 991-1002 (Marzo 2019)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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score 12.559606

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