Connecting the dots: from nanodomains to physiological functions of REMORINs

Gouguet, Paul; Gronnier, Julien; Legrand, Anthony; Perraki, Artemis; Jolivet, Marie-Dominique; Deroubaix, Anne-Flore; German-Retana, Sylvie; Boudsocq, Marie; Habenstein, Birgit; Mongrand, Sébastien; Germain, V.

doi:10.1093/plphys/kiaa063

Cited by 30 publications

(39 citation statements)

References 127 publications

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“…Some REMs and SPFH proteins have been widely used as nanodomain markers in imaging and biochemical approaches in plants. Here, we will give a brief overview of some important features of REM and SPFH proteins, for more details, readers can refer to recent reviews on this field ( Daněk et al, 2016 ; Gronnier et al, 2018 ; Gouguet et al, 2020 ). So far, REMs were the best-characterized nanodomain-resident proteins in plants.…”

Section: Nanodomain-resident Proteinsmentioning

confidence: 99%

Membrane nanodomains and transport functions in plant

Martinière

Zelazny

2021

Plant Physiology

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Far from a homogenous environment, biological membranes are highly structured with lipids and proteins segregating in domains of different sizes and dwell times. In addition, membrane are highly dynamics especially in response to environmental stimuli. Understanding the impact of the nanoscale organization of membranes on cellular functions is an outstanding question. Plant channels and transporters are tightly regulated to ensure proper cell nutrition and signaling. Increasing evidence indicates that channel and transporter nano-organization within membranes plays an important role in these regulation mechanisms. Here, we review recent advances in the field of ion, water, but also hormone transport in plants, focusing on protein organization within plasma membrane nanodomains and its cellular and physiological impacts.

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Section: Nanodomain-resident Proteinsmentioning

confidence: 99%

Membrane nanodomains and transport functions in plant

Martinière

Zelazny

2021

Plant Physiology

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“…REMORINS are plant-specific plasma membrane (PM) nanodomain markers involved in response to biotic and abiotic stresses [ 30 ]. REMORIN proteins present a highly conserved C-terminal domain and a divergent N-terminal domain and were classified into six phylogenetic groups [ 31 ].…”

Section: Introductionmentioning

confidence: 99%

StREM1.3 REMORIN Protein Plays an Agonistic Role in Potyvirus Cell-to-Cell Movement in N. benthamiana

Rocher

Simon

Jolivet

et al. 2022

Viruses

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REMORIN proteins belong to a plant-specific multigene family that localise in plasma membrane nanodomains and in plasmodesmata. We previously showed that in Nicotiana benthamiana, group 1 StREM1.3 limits the cell-to-cell spread of a potexvirus without affecting viral replication. This prompted us to check whether an effect on viral propagation could apply to potyvirus species Turnip mosaic virus (TuMV) and Potato virus A (PVA). Our results show that StREM1.3 transient or stable overexpression in transgenic lines increases potyvirus propagation, while it is slowed down in transgenic lines underexpressing endogenous NbREMs, without affecting viral replication. TuMV and PVA infection do not alter the membranous localisation of StREM1.3. Furthermore, StREM1.3-membrane anchoring is necessary for its agonist effect on potyvirus propagation. StREM1.3 phosphocode seems to lead to distinct plant responses against potexvirus and potyvirus. We also showed that StREM1.3 interacts in yeast and in planta with the key potyviral movement protein CI (cylindrical inclusion) at the level of the plasma membrane but only partially at plasmodesmata pit fields. TuMV infection also counteracts StREM1.3-induced plasmodesmata callose accumulation at plasmodesmata. Altogether, these results showed that StREM1.3 plays an agonistic role in potyvirus cell-to-cell movement in N. benthamiana.

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“…The advent of modern super-resolution light microscopy techniques [12,13] clearly showed the localization and dynamics of numerous peripheral and integral PM proteins and lipids within specific nanodomains [14][15][16][17]. However, thanks to the lack of suitable plant-optimized CLEM protocols, it is still hard to correlate these results with the immunoelectron microscopy approach.…”

Section: Introductionmentioning

confidence: 99%

Correlative Light-Environmental Scanning Electron Microscopy of Plasma Membrane Efflux Carriers of Plant Hormone Auxin

et al. 2021

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Fluorescence light microscopy provided convincing evidence for the domain organization of plant plasma membrane (PM) proteins. Both peripheral and integral PM proteins show an inhomogeneous distribution within the PM. However, the size of PM nanodomains and protein clusters is too small to accurately determine their dimensions and nano-organization using routine confocal fluorescence microscopy and super-resolution methods. To overcome this limitation, we have developed a novel correlative light electron microscopy method (CLEM) using total internal reflection fluorescence microscopy (TIRFM) and advanced environmental scanning electron microscopy (A-ESEM). Using this technique, we determined the number of auxin efflux carriers from the PINFORMED (PIN) family (NtPIN3b-GFP) within PM nanodomains of tobacco cell PM ghosts. Protoplasts were attached to coverslips and immunostained with anti-GFP primary antibody and secondary antibody conjugated to fluorochrome and gold nanoparticles. After imaging the nanodomains within the PM with TIRFM, the samples were imaged with A-ESEM without further processing, and quantification of the average number of molecules within the nanodomain was performed. Without requiring any post-fixation and coating procedures, this method allows to study details of the organization of auxin carriers and other plant PM proteins.

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Connecting the dots: from nanodomains to physiological functions of REMORINs

Cited by 30 publications

References 127 publications

Membrane nanodomains and transport functions in plant

Membrane nanodomains and transport functions in plant

StREM1.3 REMORIN Protein Plays an Agonistic Role in Potyvirus Cell-to-Cell Movement in N. benthamiana

Correlative Light-Environmental Scanning Electron Microscopy of Plasma Membrane Efflux Carriers of Plant Hormone Auxin

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