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. Viruses propagate in plants through membranous channels, called plasmodesmata, linking each cell to its neighboring cell. In this work, we challenge the role of the plasma membrane in the regulation of virus propagation. By studying the dynamics and the activation of a plant-specific protein called REMORIN, we found that the way this protein is organized inside the membrane is crucial to fulfill its function in the immunity of plants against viruses.

Wounding induces the parallel activation of two signaling cascades: a MKK4/5-MPK3/6 module (rapid) and a jasmonic acid-dependent MAP3K14-MKK3-MPK1/2/7/14 module

The Arabidopsis L-type lectin receptor-like kinase LecRK-IX.2 recruits calcium dependent protein kinases (CPKs) to phosphorylate NADPH oxidase RbohD to activate

REMORINs (REMs) are a plant-specific protein family, proposed regulators of membrane-associated molecular assemblies and well-established markers of plasma membrane nanodomains. REMs play a diverse set of functions in plant interactions with pathogens and symbionts, responses to abiotic stresses, hormone signaling and cell-to-cell communication. In this review, we highlight the established and more putative roles of REMs throughout the literature. We discuss the physiological functions of REMs, the mechanisms underlying their nanodomain-organization and their putative role as regulators of nanodomain-associated molecular assemblies. Furthermore, we discuss how REM phosphorylation may regulate their functional versatility. Overall, through data-mining and comparative analysis of the literature, we suggest how to further study the molecular mechanisms underpinning the functions of REMs.