ArticleThe New phytologist2020
Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER-PM contact sites and endocytic structures.
Article in The New phytologist, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.Biochemistry · 2026Review
- Assessing the Impact of Microwaves and Other Disruptive Pretreatments onFoods (Basel, Switzerland) · 2025Article
- Lipid droplets in plants: turnover and stress responses.Frontiers in plant science · 2025Review
- XopM, An FFAT Motif-Containing Type III Effector Protein From Xanthomonas, Suppresses MTI Responses at the Plant Plasma Membrane.Molecular plant pathology · 2024Article
- Fundamentals of redox regulation in biology.Nature reviews. Molecular cell biology · 2024Review
- Ice plant root plasma membrane aquaporins are regulated by clathrin-coated vesicles in response to salt stress.Plant physiology · 2023Article
- Exploring aquaporin functions during changes in leaf water potential.Frontiers in plant science · 2023Review
- Article
- Ubiquitin ligase OsRINGzf1 regulates drought resistance by controlling the turnover of OsPIP2;1.Plant biotechnology journal · 2022Article
- The genomic basis of the plant island syndrome in Darwin's giant daisies.Nature communications · 2022Article
- Maintaining the structural and functional homeostasis of the plant endoplasmic reticulum.Developmental cell · 2021Review
- Geometry and cellular function of organelle membrane interfaces.Plant physiology · 2021Review
- Plant NETWORKED and VAP27 Proteins Work in Complexes to Regulate Membrane-Based Functions.Contact (Thousand Oaks (Ventura County, Calif.))Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasma membrane (PM) intrinsic proteins (PIPs) are aquaporins facilitating the diffusion of water and small solutes. The functional importance of the PM organisation 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 localise 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 paralogue, 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 stabilise the aquaporins and guide their endocytosis in response to salt stress.
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