1. Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER‐PM contact sites and endocytic structures
- Author
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François Chaumont, Karolina Filik, Florencia Scochera, Pierre Morsomme, Hervé Degand, Timothée Laloux, Ana Romina Fox, Karina Alleva, and UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology
- Subjects
0106 biological sciences ,0301 basic medicine ,ENDOPLASMIC RETICULUM (ER) ,Physiology ,AQUAPORINS ,ENDOCYTOSIS ,Endocytic cycle ,endoplasmic reticulum/plasma membrane (ER/PM) contact sites (EPCSs) ,Aquaporin ,ENDOPLASMIC RETICULUM/PLASMA MEMBRANE ,plasma membrane intrinsic protein (PIP) ,Plant Science ,Aquaporins ,Endoplasmic Reticulum ,Endocytosis ,01 natural sciences ,endoplasmic reticulum–plasma membrane (ER–PM) contact sites (EPCSs) ,Protein–protein interaction ,AQUAPORIN ,purl.org/becyt/ford/1 [https] ,Ciencias Biológicas ,03 medical and health sciences ,Bimolecular fluorescence complementation ,PLANT VESICLE-ASSOCIATED MEMBRANE PROTEIN (VAMP)-ASSOCIATED PROTEIN (VAP27) ,endocytosis ,purl.org/becyt/ford/1.6 [https] ,Phylogeny ,plant vesicle‐associated membrane protein (VAMP)‐associated protein (VAP27) ,PLASMA MEMBRANE INTRINSIC PROTEIN (PIP) ,Water transport ,Full Paper ,Chemistry ,Research ,Endoplasmic reticulum ,Cell Membrane ,Full Papers ,CONCTAC SITES ,Bioquímica y Biología Molecular ,endoplasmic reticulum (ER) ,Cell biology ,aquaporin ,030104 developmental biology ,Cytoplasm ,Oocytes ,ENDOPLASMIC RETICULUM–PLASMA MEMBRANE (ER–PM) CONTACT SITES (EPCSS) ,CIENCIAS NATURALES Y EXACTAS ,010606 plant biology & botany - Abstract
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
- Published
- 2020
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