Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures
- Autores
- Fox, Ana Romina; Scochera, Florencia Paola; Laloux, Timothée; Filik, Karolina; Degand, Hervé; Morsomme, Pierre; Alleva, Karina Edith; Chaumont, François
- Año de publicación
- 2020
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Plasma membrane (PM) intrinsic proteins (PIPs) are aquaporins facilitating the diffusion of water and small solutes. The functional importance of the PM organization of PIPs in the interaction with other cellular structures is not completely understood. We performed a pull-down assay using maize (Zea mays) suspension cells expressing YFP-ZmPIP2;5 and validated the protein interactions by yeast split-ubiquitin and bimolecular fluorescence complementation assays. We expressed interacting proteins tagged with fluorescent proteins in Nicotiana benthamiana leaves and performed water transport assays in oocytes. Finally, a phylogenetic analysis was conducted. The PM located ZmPIP2;5 physically interacts with the endoplasmic reticulum (ER) resident ZmVAP27-1. This interaction requires the ZmVAP27-1 cytoplasmic major sperm domain. ZmPIP2;5 and ZmVAP27-1 localize in close vicinity in ER/PM contact sites (EPCSs) and endocytic structures upon exposure to salt stress conditions. This interaction enhances PM water permeability in oocytes. Similarly, the Arabidopsis ZmVAP27-1 paralog, AtVAP27-1, interacts with the AtPIP2;7 aquaporin. Together, these data indicate that the PIP2-VAP27 interaction in EPCSs is evolutionarily conserved, and suggest that VAP27 might stabilize the aquaporins and guide their endocytosis in response to salt stress.
Fil: Fox, Ana Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Université Catholique de Louvain; Bélgica
Fil: Scochera, Florencia Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática. Cátedra de Física; Argentina
Fil: Laloux, Timothée. Université Catholique de Louvain; Bélgica
Fil: Filik, Karolina. Université Catholique de Louvain; Bélgica
Fil: Degand, Hervé. Université Catholique de Louvain; Bélgica
Fil: Morsomme, Pierre. Université Catholique de Louvain; Bélgica
Fil: Alleva, Karina Edith. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Físico Matemática; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Chaumont, François. Université Catholique de Louvain; Bélgica - Materia
-
AQUAPORINS
ENDOCYTOSIS
ENDOPLASMIC RETICULUM/PLASMA MEMBRANE
CONCTAC SITES - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/111436
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Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structuresFox, Ana RominaScochera, Florencia PaolaLaloux, TimothéeFilik, KarolinaDegand, HervéMorsomme, PierreAlleva, Karina EdithChaumont, FrançoisAQUAPORINSENDOCYTOSISENDOPLASMIC RETICULUM/PLASMA MEMBRANECONCTAC SITEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plasma membrane (PM) intrinsic proteins (PIPs) are aquaporins facilitating the diffusion of water and small solutes. The functional importance of the PM organization of PIPs in the interaction with other cellular structures is not completely understood. We performed a pull-down assay using maize (Zea mays) suspension cells expressing YFP-ZmPIP2;5 and validated the protein interactions by yeast split-ubiquitin and bimolecular fluorescence complementation assays. We expressed interacting proteins tagged with fluorescent proteins in Nicotiana benthamiana leaves and performed water transport assays in oocytes. Finally, a phylogenetic analysis was conducted. The PM located ZmPIP2;5 physically interacts with the endoplasmic reticulum (ER) resident ZmVAP27-1. This interaction requires the ZmVAP27-1 cytoplasmic major sperm domain. ZmPIP2;5 and ZmVAP27-1 localize in close vicinity in ER/PM contact sites (EPCSs) and endocytic structures upon exposure to salt stress conditions. This interaction enhances PM water permeability in oocytes. Similarly, the Arabidopsis ZmVAP27-1 paralog, AtVAP27-1, interacts with the AtPIP2;7 aquaporin. Together, these data indicate that the PIP2-VAP27 interaction in EPCSs is evolutionarily conserved, and suggest that VAP27 might stabilize the aquaporins and guide their endocytosis in response to salt stress.Fil: Fox, Ana Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Université Catholique de Louvain; BélgicaFil: Scochera, Florencia Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática. Cátedra de Física; ArgentinaFil: Laloux, Timothée. Université Catholique de Louvain; BélgicaFil: Filik, Karolina. Université Catholique de Louvain; BélgicaFil: Degand, Hervé. Université Catholique de Louvain; BélgicaFil: Morsomme, Pierre. Université Catholique de Louvain; BélgicaFil: Alleva, Karina Edith. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Físico Matemática; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Chaumont, François. Université Catholique de Louvain; BélgicaWiley Blackwell Publishing, Inc2020-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/111436Fox, Ana Romina; Scochera, Florencia Paola; Laloux, Timothée; Filik, Karolina; Degand, Hervé; et al.; Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures; Wiley Blackwell Publishing, Inc; New Phytologist; 2020; 6-2020; 1-410028-646X1469-8137CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/nph.16743info:eu-repo/semantics/altIdentifier/url/https://nph.onlinelibrary.wiley.com/doi/10.1111/nph.16743info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:12:56Zoai:ri.conicet.gov.ar:11336/111436instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:12:56.996CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures |
title |
Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures |
spellingShingle |
Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures Fox, Ana Romina AQUAPORINS ENDOCYTOSIS ENDOPLASMIC RETICULUM/PLASMA MEMBRANE CONCTAC SITES |
title_short |
Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures |
title_full |
Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures |
title_fullStr |
Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures |
title_full_unstemmed |
Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures |
title_sort |
Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures |
dc.creator.none.fl_str_mv |
Fox, Ana Romina Scochera, Florencia Paola Laloux, Timothée Filik, Karolina Degand, Hervé Morsomme, Pierre Alleva, Karina Edith Chaumont, François |
author |
Fox, Ana Romina |
author_facet |
Fox, Ana Romina Scochera, Florencia Paola Laloux, Timothée Filik, Karolina Degand, Hervé Morsomme, Pierre Alleva, Karina Edith Chaumont, François |
author_role |
author |
author2 |
Scochera, Florencia Paola Laloux, Timothée Filik, Karolina Degand, Hervé Morsomme, Pierre Alleva, Karina Edith Chaumont, François |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
AQUAPORINS ENDOCYTOSIS ENDOPLASMIC RETICULUM/PLASMA MEMBRANE CONCTAC SITES |
topic |
AQUAPORINS ENDOCYTOSIS ENDOPLASMIC RETICULUM/PLASMA MEMBRANE CONCTAC SITES |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Plasma membrane (PM) intrinsic proteins (PIPs) are aquaporins facilitating the diffusion of water and small solutes. The functional importance of the PM organization of PIPs in the interaction with other cellular structures is not completely understood. We performed a pull-down assay using maize (Zea mays) suspension cells expressing YFP-ZmPIP2;5 and validated the protein interactions by yeast split-ubiquitin and bimolecular fluorescence complementation assays. We expressed interacting proteins tagged with fluorescent proteins in Nicotiana benthamiana leaves and performed water transport assays in oocytes. Finally, a phylogenetic analysis was conducted. The PM located ZmPIP2;5 physically interacts with the endoplasmic reticulum (ER) resident ZmVAP27-1. This interaction requires the ZmVAP27-1 cytoplasmic major sperm domain. ZmPIP2;5 and ZmVAP27-1 localize in close vicinity in ER/PM contact sites (EPCSs) and endocytic structures upon exposure to salt stress conditions. This interaction enhances PM water permeability in oocytes. Similarly, the Arabidopsis ZmVAP27-1 paralog, AtVAP27-1, interacts with the AtPIP2;7 aquaporin. Together, these data indicate that the PIP2-VAP27 interaction in EPCSs is evolutionarily conserved, and suggest that VAP27 might stabilize the aquaporins and guide their endocytosis in response to salt stress. Fil: Fox, Ana Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Université Catholique de Louvain; Bélgica Fil: Scochera, Florencia Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Fisicomatemática. Cátedra de Física; Argentina Fil: Laloux, Timothée. Université Catholique de Louvain; Bélgica Fil: Filik, Karolina. Université Catholique de Louvain; Bélgica Fil: Degand, Hervé. Université Catholique de Louvain; Bélgica Fil: Morsomme, Pierre. Université Catholique de Louvain; Bélgica Fil: Alleva, Karina Edith. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Físico Matemática; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina Fil: Chaumont, François. Université Catholique de Louvain; Bélgica |
description |
Plasma membrane (PM) intrinsic proteins (PIPs) are aquaporins facilitating the diffusion of water and small solutes. The functional importance of the PM organization of PIPs in the interaction with other cellular structures is not completely understood. We performed a pull-down assay using maize (Zea mays) suspension cells expressing YFP-ZmPIP2;5 and validated the protein interactions by yeast split-ubiquitin and bimolecular fluorescence complementation assays. We expressed interacting proteins tagged with fluorescent proteins in Nicotiana benthamiana leaves and performed water transport assays in oocytes. Finally, a phylogenetic analysis was conducted. The PM located ZmPIP2;5 physically interacts with the endoplasmic reticulum (ER) resident ZmVAP27-1. This interaction requires the ZmVAP27-1 cytoplasmic major sperm domain. ZmPIP2;5 and ZmVAP27-1 localize in close vicinity in ER/PM contact sites (EPCSs) and endocytic structures upon exposure to salt stress conditions. This interaction enhances PM water permeability in oocytes. Similarly, the Arabidopsis ZmVAP27-1 paralog, AtVAP27-1, interacts with the AtPIP2;7 aquaporin. Together, these data indicate that the PIP2-VAP27 interaction in EPCSs is evolutionarily conserved, and suggest that VAP27 might stabilize the aquaporins and guide their endocytosis in response to salt stress. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-06 |
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/11336/111436 Fox, Ana Romina; Scochera, Florencia Paola; Laloux, Timothée; Filik, Karolina; Degand, Hervé; et al.; Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures; Wiley Blackwell Publishing, Inc; New Phytologist; 2020; 6-2020; 1-41 0028-646X 1469-8137 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/111436 |
identifier_str_mv |
Fox, Ana Romina; Scochera, Florencia Paola; Laloux, Timothée; Filik, Karolina; Degand, Hervé; et al.; Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures; Wiley Blackwell Publishing, Inc; New Phytologist; 2020; 6-2020; 1-41 0028-646X 1469-8137 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1111/nph.16743 info:eu-repo/semantics/altIdentifier/url/https://nph.onlinelibrary.wiley.com/doi/10.1111/nph.16743 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844614041054478336 |
score |
13.070432 |