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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/111436
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/111436
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T11:42:51Zoai: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:34982025-10-22 11:42:51.308CONICET 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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score 12.982451

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