Membrane nanodomains and transport functions in plant

Martinière, Alexandre; Zelazny, Enric

doi:10.1093/plphys/kiab312

Cited by 18 publications

(20 citation statements)

References 158 publications

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“…CWLP and PRP940 display clustered co-localization in the PM with aquaporin PIP2;1 in nanodomains (103). Our study confirms that C-terminal 8CM domains of both proteins are preprint (which was not certified by peer review) is the author/funder.…”

Section: Cw-pm Linker Functions Of Cwlp and Prp940supporting

confidence: 75%

“…6E). These results indicated that CWLP and PRP940 form aquaporin complexes independently of FLOT2 in distinct nanodomains and thus revealed a novel class of PM-ND complexes (25,103,127).…”

Section: Aquaporin Binding and Recruitment Of Pp2a Phosphatase B''-su...mentioning

confidence: 83%

“…CWLP and PRP940 display clustered co-localization in the PM with aquaporin PIP2;1 in nanodomains (103). Our study confirms that C-terminal 8CM domains of both proteins are closely related to 8CMs of Hydrophobic Protein from Soybean (PDB entry 1HYP; 94) and nsLTP proteins, which form tunnel-like lipid-binding cavities and might function as PM anchors.…”

Section: Discussionmentioning

confidence: 99%

“…1G). This observation indicated that part of CWLP is present in nanodomainderived DRMs, but also detectable in the TSM and Sup fractions, likely due to the dynamic equilibrium between PM-trafficking, clustering, and recycling of these nanodomain proteins (100,101,(103)(104)(105).…”

Section: Verification Of Glycosylation Nanodomain Anchoring and Cell ...mentioning

confidence: 94%

“…Co-localization of CWLP and PRP940 with PIP2;1 (Fig. 1B) in PM clusters thus suggested that CWLP and PRP940 are localized in PIP2;1marked PM-NDs, which are composed of "detergent-resistant membranes" (DRMs) that cannot be entirely solubilized by the nonionic detergent Triton X-100 at low temperature (101)(102)(103). To confirm that CWLP is a DRM-associated protein, total cell extract from CWLP-GFPexpressing 15-d-old seedlings was fractionated to cleared (100,000 g) supernatant (Sup), Triton X-100 solubilized (TSM), and DRM protein fractions and analyzed by western blotting using anti-GFP Ab (Fig.…”

Section: Verification Of Glycosylation Nanodomain Anchoring and Cell ...mentioning

confidence: 99%

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CWLP and PRP940 form plasma-membrane nanodomain complexes with aquaporins, interact with PP2A and contribute to dehydration tolerance

Honig

Eilenberg

Zuther

et al. 2022

Preprint

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The C-type hybrid-proline-rich protein (HyPRP) AtCWLP and its homolog AtPRP940 are referred as cell wall (CW)-plasma-membrane (PM) linker proteins, but little is known about their functions. Here we show that N-terminal proline-rich domains of CWLP and PRP940, containing glycosylated hydroxyproline residues, contact the CW, while their C-terminal 8CM domains function as PM-scaffolds. Both proteins are detected in PM nanodomains (PM-ND) and show co-localization and co-immunoprecipitation with aquaporins PIP2;1 and PIP2;7. Inhibition of actin polymerization by latrunculin B promotes CWLP-endosome appearance, while blocking the actomyosin-based transport by a truncated form of myosin XI-K relaxes lateral boundaries of CWLP-PIP2;1 PD-NDs. Mass spectrometry data indicate that CWLP co-purifies with dynamins implicated in fission of endocytic PD-ND invaginations. Lack of co-localization and co-immunoprecipitation with aquaporin-binding flotillin (FLOT2) indicates that CWLP and PRP940 mark a new distinct type of PM-ND. Yeast two-hybrid and co-immunoprecipitation assays demonstrate that CWLP and PRP940 interact with multiple aquaporins and several protein phosphatase PP2A-B’’ regulatory subunits. By preventing irreversible separation of CW and PM, and likely assisting PP2A-mediated dephosphorylation of aquaporins and closure of their water channels, overexpression of CWLP confers tolerance to plasmolysis, dehydration and freezing in Arabidopsis and to water shortage in potato plants.Summary StatementArabidopsis Hybrid-Proline-Rich Proteins CWLP and PRP940 occur in association with dynamins, recruit PP2A protein phosphatases to aquaporin water channels in plasma-membrane (PM) nanodomains and elevate tolerance to cellular dehydration.

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Section: Cw-pm Linker Functions Of Cwlp and Prp940supporting

confidence: 75%

“…6E). These results indicated that CWLP and PRP940 form aquaporin complexes independently of FLOT2 in distinct nanodomains and thus revealed a novel class of PM-ND complexes (25,103,127).…”

Section: Aquaporin Binding and Recruitment Of Pp2a Phosphatase B''-su...mentioning

confidence: 83%

Section: Discussionmentioning

confidence: 99%

Section: Verification Of Glycosylation Nanodomain Anchoring and Cell ...mentioning

confidence: 94%

Section: Verification Of Glycosylation Nanodomain Anchoring and Cell ...mentioning

confidence: 99%

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CWLP and PRP940 form plasma-membrane nanodomain complexes with aquaporins, interact with PP2A and contribute to dehydration tolerance

Honig

Eilenberg

Zuther

et al. 2022

Preprint

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Interplay between membrane proteins and membrane protein‐lipid pertaining to plant salinity stress

Dutta

2023

Cell Biochemistry & Function

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High salinity in agricultural lands is one of the predominant issues limiting agricultural yields. Plants have developed several mechanisms to withstand salinity stress, but the mechanisms are not effective enough for most crops to prevent and persist the salinity stress. Plant salt tolerance pathways involve membrane proteins that have a crucial role in sensing and mitigating salinity stress. Due to a strategic location interfacing two distinct cellular environments, membrane proteins can be considered checkpoints to the salt tolerance pathways in plants. Related membrane proteins functions include ion homeostasis, osmosensing or ion sensing, signal transduction, redox homeostasis, and small molecule transport. Therefore, modulating plant membrane proteins' function, expression, and distribution can improve plant salt tolerance. This review discusses the membrane protein–protein and protein–lipid interactions related to plant salinity stress. It will also highlight the finding of membrane protein–lipid interactions from the context of recent structural evidence. Finally, the importance of membrane protein–protein and protein–lipid interaction is discussed, and a future perspective on studying the membrane protein–protein and protein–lipid interactions to develop strategies for improving salinity tolerance is proposed.

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Cross-regulation of cytoskeleton and calcium signaling at plant-pathogen interface

Naveed,

Jamil,

Asif

et al. 2024

Cellular Signalling

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Membrane nanodomains and transport functions in plant

Cited by 18 publications

References 158 publications

CWLP and PRP940 form plasma-membrane nanodomain complexes with aquaporins, interact with PP2A and contribute to dehydration tolerance

CWLP and PRP940 form plasma-membrane nanodomain complexes with aquaporins, interact with PP2A and contribute to dehydration tolerance

Interplay between membrane proteins and membrane protein‐lipid pertaining to plant salinity stress

Cross-regulation of cytoskeleton and calcium signaling at plant-pathogen interface

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