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resumen

Resumen
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 [ver mas...]
dc.contributor.authorVitali, Victoria Andrea
dc.contributor.authorJozefkowicz, Cintia
dc.contributor.authorCanessa Fortuna, Agustina
dc.contributor.authorSoto, Gabriela Cinthia
dc.contributor.authorGonzalez Flecha, Francisco Luis
dc.contributor.authorAlleva, Karina Edith
dc.date.accessioned2019-05-03T16:42:26Z
dc.date.available2019-05-03T16:42:26Z
dc.date.issued2019-03
dc.identifier.issn1742-464X
dc.identifier.otherhttps://doi.org/10.1111/febs.14701
dc.identifier.urihttps://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.14701
dc.identifier.urihttp://hdl.handle.net/20.500.12123/5031
dc.description.abstractOne 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.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherWileyes_AR
dc.rightsinfo:eu-repo/semantics/restrictedAccesses_AR
dc.sourceThe Febs journal 286 (5) : 991-1002 (Marzo 2019)es_AR
dc.subjectPlant Water Relationseng
dc.subjectRelaciones Planta Aguaes_AR
dc.subjectCell Membraneseng
dc.subjectMembranas Celulareses_AR
dc.subject.otherAquaporineng
dc.subject.otherAcuaporinases_AR
dc.titleCooperativity in proton sensing by PIP aquaporinses_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/publishedVersiones_AR
dc.description.origenInstituto de Genéticaes_AR
dc.description.filFil: 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; Argentinaes_AR
dc.description.filFil: Jozefkowicz, Cintia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: 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; Argentinaes_AR
dc.description.filFil: Soto, Gabriela Cinthia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: 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.es_AR
dc.description.filFil: 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; Argentinaes_AR
dc.subtypecientifico


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