Pip water transport and its pH dependence are regulated by tetramer stoichiometry
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 biologica...
| Autores principales: | , , , , , , , , |
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| Formato: | info:eu-repo/semantics/article |
| Lenguaje: | Inglés |
| Publicado: |
2017
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| Materias: | |
| Acceso en línea: | 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 |
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| author | 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_browse | Alleva, Karina Edith Amodeo, Gabriela Ayub, Nicolás Daniel Gonzalez Flecha, Francisco Luis Jozefkowicz, Cintia Pietrasanta, Lía Isabel Scochera, Florencia Sigaut, Lorena Soto, Gabriela Cinthia |
| 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_sort | Jozefkowicz, Cintia |
| collection | INTA Digital |
| 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. |
| format | info:eu-repo/semantics/article |
| id | INTA1083 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2017 |
| publishDateRange | 2017 |
| publishDateSort | 2017 |
| record_format | dspace |
| spelling | INTA10832018-08-06T18:29:24Z Pip water transport and its pH dependence are regulated by tetramer stoichiometry Jozefkowicz, Cintia Sigaut, Lorena Scochera, Florencia Soto, Gabriela Cinthia Ayub, Nicolás Daniel Pietrasanta, Lía Isabel Amodeo, Gabriela Gonzalez Flecha, Francisco Luis Alleva, Karina Edith Agua Ph Membranas Celulares Water Cell Membranes 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 2017-08-30T15:15:22Z 2017-08-30T15:15:22Z 2016 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion info:ar-repo/semantics/artículo 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 eng 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) application/pdf Biophysical Journal 110 (6) :1312-1321. (March 2016) |
| spellingShingle | Agua Ph Membranas Celulares Water Cell Membranes Jozefkowicz, Cintia Sigaut, Lorena Scochera, Florencia Soto, Gabriela Cinthia Ayub, Nicolás Daniel Pietrasanta, Lía Isabel Amodeo, Gabriela Gonzalez Flecha, Francisco Luis Alleva, Karina Edith 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 |
| 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_short | 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 |
| topic | Agua Ph Membranas Celulares Water Cell Membranes |
| 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 |
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