Cooperativity in proton sensing by PIP aquaporins
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, u...
| Main Authors: | , , , , , |
|---|---|
| Format: | info:ar-repo/semantics/artículo |
| Language: | Inglés |
| Published: |
Wiley
2019
|
| Subjects: | |
| Online Access: | 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 |
| _version_ | 1855035426663825408 |
|---|---|
| author | Vitali, Victoria Andrea Jozefkowicz, Cintia Canessa Fortuna, Agustina Soto, Gabriela Cinthia Gonzalez Flecha, Francisco Luis Alleva, Karina Edith |
| author_browse | Alleva, Karina Edith Canessa Fortuna, Agustina Gonzalez Flecha, Francisco Luis Jozefkowicz, Cintia Soto, Gabriela Cinthia Vitali, Victoria Andrea |
| author_facet | Vitali, Victoria Andrea Jozefkowicz, Cintia Canessa Fortuna, Agustina Soto, Gabriela Cinthia Gonzalez Flecha, Francisco Luis Alleva, Karina Edith |
| author_sort | Vitali, Victoria Andrea |
| collection | INTA Digital |
| 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. |
| format | info:ar-repo/semantics/artículo |
| id | INTA5031 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2019 |
| publishDateRange | 2019 |
| publishDateSort | 2019 |
| publisher | Wiley |
| publisherStr | Wiley |
| record_format | dspace |
| spelling | INTA50312019-05-03T18:43:53Z Cooperativity in proton sensing by PIP aquaporins Vitali, Victoria Andrea Jozefkowicz, Cintia Canessa Fortuna, Agustina Soto, Gabriela Cinthia Gonzalez Flecha, Francisco Luis Alleva, Karina Edith Plant Water Relations Cell Membranes Relaciones Planta Agua Membranas Celulares Aquaporin Acuaporinas 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 2019-05-03T16:42:26Z 2019-05-03T16:42:26Z 2019-03 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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 eng info:eu-repo/semantics/restrictedAccess application/pdf Wiley The Febs journal 286 (5) : 991-1002 (Marzo 2019) |
| spellingShingle | Plant Water Relations Cell Membranes Relaciones Planta Agua Membranas Celulares Aquaporin Acuaporinas Vitali, Victoria Andrea Jozefkowicz, Cintia Canessa Fortuna, Agustina Soto, Gabriela Cinthia Gonzalez Flecha, Francisco Luis Alleva, Karina Edith Cooperativity in proton sensing by PIP aquaporins |
| title | 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_short | Cooperativity in proton sensing by PIP aquaporins |
| title_sort | cooperativity in proton sensing by pip aquaporins |
| topic | Plant Water Relations Cell Membranes Relaciones Planta Agua Membranas Celulares Aquaporin Acuaporinas |
| 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 |
| work_keys_str_mv | AT vitalivictoriaandrea cooperativityinprotonsensingbypipaquaporins AT jozefkowiczcintia cooperativityinprotonsensingbypipaquaporins AT canessafortunaagustina cooperativityinprotonsensingbypipaquaporins AT sotogabrielacinthia cooperativityinprotonsensingbypipaquaporins AT gonzalezflechafranciscoluis cooperativityinprotonsensingbypipaquaporins AT allevakarinaedith cooperativityinprotonsensingbypipaquaporins |