Pip water transport and its pH dependence are regulated by tetramer stoichiometry

Autores
Jozefkowicz, Cintia; Sigaut, Lorena; Scochera, Florencia; Soto, Gabriela Cinthia; Ayub, Nicolás Daniel; Pietrasanta, Lía Isabel; Amodeo, Gabriela; Gonzalez Flecha, Francisco Luis; Alleva, Karina Edith
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 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.
Inst. de Genética "Ewald A. Favret"- IGEAF
Fil: 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
Fil: Sigaut, Lorena. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Microscopías Avanzadas; Argentina
Fil: 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
Fil: Soto, Gabriela Cinthia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina
Fil: Ayub, Nicolás Daniel. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina
Fil: 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
Fil: 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
Fil: 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
Fil: 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
Fuente
Biophysical Journal 110 (6) :1312-1321. (March 2016)
Materia
Agua
Ph
Membranas Celulares
Water
Cell Membranes
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/1083
Acceder
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oai_identifier_str oai:localhost:20.500.12123/1083
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network_name_str INTA Digital (INTA)
spelling Pip water transport and its pH dependence are regulated by tetramer stoichiometryJozefkowicz, CintiaSigaut, LorenaScochera, FlorenciaSoto, Gabriela CinthiaAyub, Nicolás DanielPietrasanta, Lía IsabelAmodeo, GabrielaGonzalez Flecha, Francisco LuisAlleva, Karina EdithAguaPhMembranas CelularesWaterCell MembranesMany 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.Inst. de Genética "Ewald A. Favret"- IGEAFFil: 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; ArgentinaFil: Sigaut, Lorena. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Microscopías Avanzadas; ArgentinaFil: 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; ArgentinaFil: Soto, Gabriela Cinthia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; ArgentinaFil: Ayub, Nicolás Daniel. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; ArgentinaFil: 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; ArgentinaFil: 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; ArgentinaFil: 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; ArgentinaFil: 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; Argentina2017-08-30T15:15:22Z2017-08-30T15:15:22Z2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/1083http://ac.els-cdn.com/S0006349516001351/1-s2.0-S0006349516001351-main.pdf?_tid=da62a74e-8d97-11e7-b453-00000aacb361&acdnat=1504107080_124ed9f2ea10addd83bfe98d746c19210006-3495 (Print)1542-0086 (Online)https://doi.org/10.1016/j.bpj.2016.01.026Biophysical Journal 110 (6) :1312-1321. (March 2016)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2025-09-04T09:46:58Zoai:localhost:20.500.12123/1083instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-04 09:46:59.271INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Pip water transport and its pH dependence are regulated by tetramer stoichiometry
title Pip water transport and its pH dependence are regulated by tetramer stoichiometry
spellingShingle Pip water transport and its pH dependence are regulated by tetramer stoichiometry
Jozefkowicz, Cintia
Agua
Ph
Membranas Celulares
Water
Cell Membranes
title_short Pip water transport and its pH dependence are regulated by tetramer stoichiometry
title_full Pip water transport and its pH dependence are regulated by tetramer stoichiometry
title_fullStr Pip water transport and its pH dependence are regulated by tetramer stoichiometry
title_full_unstemmed Pip water transport and its pH dependence are regulated by tetramer stoichiometry
title_sort Pip water transport and its pH dependence are regulated by tetramer stoichiometry
dc.creator.none.fl_str_mv Jozefkowicz, Cintia
Sigaut, Lorena
Scochera, Florencia
Soto, Gabriela Cinthia
Ayub, Nicolás Daniel
Pietrasanta, Lía Isabel
Amodeo, Gabriela
Gonzalez Flecha, Francisco Luis
Alleva, Karina Edith
author Jozefkowicz, Cintia
author_facet Jozefkowicz, Cintia
Sigaut, Lorena
Scochera, Florencia
Soto, Gabriela Cinthia
Ayub, Nicolás Daniel
Pietrasanta, Lía Isabel
Amodeo, Gabriela
Gonzalez Flecha, Francisco Luis
Alleva, Karina Edith
author_role author
author2 Sigaut, Lorena
Scochera, Florencia
Soto, Gabriela Cinthia
Ayub, Nicolás Daniel
Pietrasanta, Lía Isabel
Amodeo, Gabriela
Gonzalez Flecha, Francisco Luis
Alleva, Karina Edith
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Agua
Ph
Membranas Celulares
Water
Cell Membranes
topic Agua
Ph
Membranas Celulares
Water
Cell Membranes
dc.description.none.fl_txt_mv 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 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.
Inst. de Genética "Ewald A. Favret"- IGEAF
Fil: 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
Fil: Sigaut, Lorena. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Microscopías Avanzadas; Argentina
Fil: 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
Fil: Soto, Gabriela Cinthia. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina
Fil: Ayub, Nicolás Daniel. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Genética; Argentina
Fil: 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
Fil: 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
Fil: 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
Fil: 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
description 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 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.
publishDate 2016
dc.date.none.fl_str_mv 2016
2017-08-30T15:15:22Z
2017-08-30T15:15:22Z
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/20.500.12123/1083
http://ac.els-cdn.com/S0006349516001351/1-s2.0-S0006349516001351-main.pdf?_tid=da62a74e-8d97-11e7-b453-00000aacb361&acdnat=1504107080_124ed9f2ea10addd83bfe98d746c1921
0006-3495 (Print)
1542-0086 (Online)
https://doi.org/10.1016/j.bpj.2016.01.026
url http://hdl.handle.net/20.500.12123/1083
http://ac.els-cdn.com/S0006349516001351/1-s2.0-S0006349516001351-main.pdf?_tid=da62a74e-8d97-11e7-b453-00000aacb361&acdnat=1504107080_124ed9f2ea10addd83bfe98d746c1921
https://doi.org/10.1016/j.bpj.2016.01.026
identifier_str_mv 0006-3495 (Print)
1542-0086 (Online)
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Biophysical Journal 110 (6) :1312-1321. (March 2016)
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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