Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains

Abstract

Plasma Membrane is the primary structure for adjusting to ever changing conditions. PM sub-compartmentalization in domains is thought to orchestrate signaling. Yet, mechanisms governing membrane organization are mostly uncharacterized. The plant-specific REMORINs are proteins regulating hormonal crosstalk and host invasion. REMs are the best-characterized nanodomain markers via an uncharacterized moiety called REMORIN C-terminal Anchor. By coupling biophysical methods, super-resolution microscopy and physiology, we decipher an original mechanism regulating the dynamic and organization of nanodomains. We showed that targeting of REMORIN is independent of the COP-II-dependent secretory pathway and mediated by PI4P and sterol. REM-CA is an unconventional lipid-binding motif that confers nanodomain organization. Analyses of REM-CA mutants by single particle tracking demonstrate that mobility and supramolecular organization are critical for immunity. This study provides a unique mechanistic insight into how the tight control of spatial segregation is critical in the definition of PM domain necessary to support biological function.DOI: http://dx.doi.org/10.7554/eLife.26404.001

Remorin interacting with PCaP1 impairs Turnip mosaic virus intercellular movement but is antagonised by VPg

“…REM1.2 and REM1.3 isoforms are expressed at more than 20‐fold higher levels compared with any other members of the REM multigenic family (Jarsch et al ., ). REM1.2 and REM1.3 localise to the same PM nanodomain (Demir et al ., ; Bücherl et al ., ) and share the same pattern of S ‐acylation (Hemsley et al ., ; Konrad et al ., ) or phosphorylation (Mehlmer et al ., ; Marin & Ott, ; Perraki et al ., ) and might function similarly as described previously (Keinath et al ., ; Gronnier et al ., ; Perraki et al ., ). Therefore, we mainly focused on REM1.2 for further analysis.…”

“…Recently, group 1 Remorins (REMs) have been shown to be involved in virus cell-to-cell movement. REMs are plant-specific nanodomain-organised proteins of the inner-leaflet of the PM (Raffaele et al, 2007(Raffaele et al, , 2009Jarsch et al, 2014;Konrad et al, 2014;Gronnier et al, 2017). Overexpression of potato StREM1.3 impairs the cell-to-cell movement of PVX and TMV (Raffaele et al, 2009;Perraki et al, 2018), while transient overexpression of Arabidopsis AtREM1.2 (REM1.2) or AtREM1.3 (REM1.3) impairs the cell-to-cell movement of PVX (Perraki et al, 2018).…”

Phosphorylation-dependent routing of RLP44 towards brassinosteroid or phytosulfokine signalling

“…Thus, the multitude of potential interactions and extensive sharing of components between pathways, raise a central question in plant signal transduction: how can distinct signalling responses be achieved? A partial answer is provided by the discovery of membrane sub-compartmentalization that helps to spatially separate potential interaction partners (Jarsch et al, 2014, Wang et al, 2015b, Bucherl et al, 2017, Gronnier et al, 2017, Ott, 2017. Furthermore, selective endocytosis, recycling, and eventually, the degradation of RLKs in the vacuole (Martins et al, 2015, Mbengue et al, 2016, Zhou et al, 2018 are crucial for tuning of signalling.…”

Avidity‐driven polarity establishment via multivalent lipid– GTP ase module interactions

“…This is likely to reduce the diffusion of Cdc42 GTPase components locally. In eukaryotes, diverse Ras-family GTPases display heterogeneous diffusion on the plasma membrane, where active GTPases and other signaling proteins have been imaged in discrete subdiffraction limited ensembles, also referred to as nanoclusters (Murakoshi et al, 2004;Tian et al, 2007;Das et al, 2015;Nan et al, 2015;Zhou et al, 2015Zhou et al, , 2017Gronnier et al, 2017;Remorino et al, 2017). Cdc42 is organized in nanoclusters that are larger at the cell pole (Sartorel et al, 2018), where Bem1 contributes to GTPase activation (Rapali et al, 2017).…”