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Abstract
Many plasma membrane channels form oligomeric assemblies, and heterooligomerization has been described as a distinctive feature of some protein families. In the particular case of plant plasma membrane aquaporins (PIPs), PIP1 and PIP2 monomers interact to form heterotetramers. However, the biological properties of the different heterotetrameric configurations formed by PIP1 and PIP2 subunits have not been addressed yet. Upon coexpression of tandem [ver mas...]
dc.contributor.authorJozefkowicz, Cintia
dc.contributor.authorSigaut, Lorena
dc.contributor.authorScochera, Florencia
dc.contributor.authorSoto, Gabriela Cinthia
dc.contributor.authorAyub, Nicolás Daniel
dc.contributor.authorPietrasanta, Lía Isabel
dc.contributor.authorAmodeo, Gabriela
dc.contributor.authorGonzalez Flecha, Francisco Luis
dc.contributor.authorAlleva, Karina Edith
dc.date.accessioned2017-08-30T15:15:22Z
dc.date.available2017-08-30T15:15:22Z
dc.date.issued2016
dc.identifier.issn0006-3495 (Print)
dc.identifier.issn1542-0086 (Online)
dc.identifier.otherhttps://doi.org/10.1016/j.bpj.2016.01.026
dc.identifier.urihttp://hdl.handle.net/20.500.12123/1083
dc.identifier.urihttp://ac.els-cdn.com/S0006349516001351/1-s2.0-S0006349516001351-main.pdf?_tid=da62a74e-8d97-11e7-b453-00000aacb361&acdnat=1504107080_124ed9f2ea10addd83bfe98d746c1921
dc.description.abstractMany plasma membrane channels form oligomeric assemblies, and heterooligomerization has been described as a distinctive feature of some protein families. In the particular case of plant plasma membrane aquaporins (PIPs), PIP1 and PIP2 monomers interact to form heterotetramers. However, the biological properties of the different heterotetrameric configurations formed by PIP1 and PIP2 subunits have not been addressed yet. Upon coexpression of tandem PIP2-PIP1 dimers in Xenopus oocytes, we can address, for the first time to our knowledge, the functional properties of single heterotetrameric species having 2:2 stoichiometry. We have also coexpressed PIP2-PIP1 dimers with PIP1 and PIP2 monomers to experimentally investigate the localization and biological activity of each tetrameric assembly. Our results show that PIP2-PIP1 heterotetramers can assemble with 3:1, 1:3, or 2:2 stoichiometry, depending on PIP1 and PIP2 relative expression in the cell. All PIP2-PIP1 heterotetrameric species localize at the plasma membrane and present the same water transport capacity. Furthermore, the contribution of any heterotetrameric assembly to the total water transport through the plasma membrane doubles the contribution of PIP2 homotetramers. Our results also indicate that plasma membrane water transport can be modulated by the coexistence of different tetrameric species and by intracellular pH. Moreover, all the tetrameric species present similar cooperativity behavior for proton sensing. These findings throw light on the functional properties of PIP tetramers, showing that they have flexible stoichiometry dependent on the quantity of PIP1 and PIP2 molecules available. This represents, to our knowledge, a novel regulatory mechanism to adjust water transport across the plasma membrane.
dc.formatapplication/pdfeng
dc.language.isoeng
dc.rightsinfo:eu-repo/semantics/openAccesseng
dc.sourceBiophysical Journal 110 (6) :1312-1321. (March 2016)
dc.subjectAgua
dc.subjectWatereng
dc.subjectPh
dc.subjectMembranas Celulares
dc.subjectCell Membraneseng
dc.titlePip water transport and its pH dependence are regulated by tetramer stoichiometryeng
dc.typeinfo:eu-repo/semantics/articleeng
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersioneng
dc.description.origenInst. de Genética "Ewald A. Favret"- IGEAF
dc.gic151768
dc.description.filFil: Jozefkowicz, Cintia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.filFil: Sigaut, Lorena. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Microscopías Avanzadas; Argentina
dc.description.filFil: Scochera, Florencia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina. Universidad de Buenos Aires, Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; Argentina
dc.description.filFil: Soto, Gabriela Cinthia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina
dc.description.filFil: Ayub, Nicolás Daniel. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina
dc.description.filFil: Pietrasanta, Lia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Microscopías Avanzadas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.filFil: Amodeo, Gabriela. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biologia Experimental y Aplicada; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina
dc.description.filFil: Gonzalez Flecha, Francisco Luis. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina; Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.filFil: Alleva, Karina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina. Universidad de Buenos Aires, Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática; Argentina
dc.subtypecientifico


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