Research Article: REM1.3’s phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement

Date Published: November 12, 2018

Publisher: Public Library of Science

Author(s): Artemis Perraki, Julien Gronnier, Paul Gouguet, Marie Boudsocq, Anne-Flore Deroubaix, Vincent Simon, Sylvie German-Retana, Anthony Legrand, Birgit Habenstein, Cyril Zipfel, Emmanuelle Bayer, Sébastien Mongrand, Véronique Germain, Aiming Wang.


Plants respond to pathogens through dynamic regulation of plasma membrane-bound signaling pathways. To date, how the plant plasma membrane is involved in responses to viruses is mostly unknown. Here, we show that plant cells sense the Potato virus X (PVX) COAT PROTEIN and TRIPLE GENE BLOCK 1 proteins and subsequently trigger the activation of a membrane-bound calcium-dependent kinase. We show that the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3-interacts with group 1 REMORINs in vivo, phosphorylates the intrinsically disordered N-terminal domain of the Group 1 REMORIN REM1.3, and restricts PVX cell-to-cell movement. REM1.3’s phospho-status defines its plasma membrane nanodomain organization and is crucial for REM1.3-dependent restriction of PVX cell-to-cell movement by regulation of callose deposition at plasmodesmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses.

Partial Text

The cell plasma membrane (PM) constitutes a regulatory hub for information processing [1]. Current knowledge suggests that PM proteins and lipids dynamically associate with each other to create specialized sub-compartments or nanodomains [2], that regulate the cellular responses in space and time [3–5]. For instance, modeling of the localization behavior of a PM-bound receptor and its downstream interactor before and after ligand perception in animal cells suggests that PM-partitioning into nanodomains improves the reliability of cell signaling [6]. In plants a recent example of PM partitioning shows that despite sharing several signaling components, the immune and growth receptors FLS2 and BRI1 are divided into context-specific nanodomains to confer signaling specificity [7]. The REMORIN (REM) family is one of the best-characterized PM nanodomain-associated proteins in plants [7–12]. The association of REMs to the PM is mediated by a short sequence at the extremity of the C-terminus of the protein, called REM-CA (REMORIN C-terminal Anchor) [13, 14]. The REM C-terminal domain contains a coiled-coil (residues 117–152, [15]) which is thought to regulate REM oligomerization [11, 14, 16] and may be involved in regulating REM spatial organization at the PM [15]. Members of the REM family have been associated with plant responses to biotic [9, 17, 18], abiotic stress [19, 20] and developmental clues [12] and current view suggests they could regulate signaling events through nanodomain association [21]. However, the molecular mechanisms leading to REM-associated downstream events remain elusive.

Protein phosphorylation is a ubiquitous and specific mechanism of cell communication [75]. The addition of a phosphate group on one or more critical residues of a given protein can induce important conformational changes that affect energetically favorable interactions and may lead to changes in its interacting network, localization, abundance and may influence the activity of protein signaling pools [76]. Although, since the initial discovery of REM1.3 in 1989, accumulating evidence suggests that the functions of REM proteins are regulated by protein phosphorylation [38–40]. The biological significance of this phosphorylation remained unclear to this date. REM proteins were among the first plant proteins described which supported the notion of PM sub-compartmentalization to functional protein-lipid nanodomains [8, 11, 77], also named membrane rafts [3, 4, 21]. In the present paper, we used REM1.3 and PVX as an experimental system to study the role of protein phosphorylation and membrane dynamics in the context of stress response.




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