In:
New Phytologist, Wiley, Vol. 228, No. 3 ( 2020-11), p. 973-988
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‐ Zm PIP2;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 Zm PIP2;5 physically interacts with the endoplasmic reticulum (ER) resident Zm VAP27‐1. This interaction requires the Zm VAP27‐1 cytoplasmic major sperm domain. Zm PIP2;5 and Zm VAP27‐1 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 Zm VAP27‐1 paralogue, At VAP27‐1, interacts with the At PIP2;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.
Type of Medium:
Online Resource
ISSN:
0028-646X
,
1469-8137
Language:
English
Publisher:
Wiley
Publication Date:
2020
detail.hit.zdb_id:
208885-X
detail.hit.zdb_id:
1472194-6
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