Abstract
Plasma membranes provide a highly selective environment for a large number of transmembrane and membrane-associated proteins. Whereas lateral movement of proteins in this lipid bilayer is possible, it is rather limited in turgid and cell wall-shielded plant cells. However, membrane-resident signaling processes occur on subsecond scales that cannot be explained by simple diffusion models. Accordingly, several receptors and other membrane-associated proteins are organized and functional in membrane nanodomains. Although the general presence of membrane nanodomains has become widely accepted as fact, fundamental functional aspects, the roles of individual lipid species and their interplay with proteins, and aspects of nanodomain maintenance and persistence remain poorly understood. Here, we review the current knowledge of nanodomain organization and function, with a particular focus on signaling processes involving proteins, lipids, and their interactions. Furthermore, we propose new and hypothetical aspects of plant membrane biology that we consider important for future research.
Highlights
Together with the cell wall, the plasma membrane forms the frontier of the cell
We review the current evidence for the coexistence of a patchwork of membrane nanodomains in the plant plasma membrane and their functional importance and assess the roles of lipids, the cell wall and the cytoskeleton in shaping this diverse plasma membrane landscape
CONCLUDING REMARKS AND PERSPECTIVES Altogether, accumulating evidence over the last years clearly demonstrates that the plant plasma membrane, like the plasma membrane in other eukaryotic cells, is highly compartmentalized
Summary
Receptor-scaffolding at the nanoscale Unequivocal evidence demonstrates that a significant number of membrane-resident proteins cluster in higher order structures that have been termed ‘membrane nanodomains’ or ‘membrane microdomains’, for which a nomenclature has been suggested recently (Ott, 2017). Members of the flotillin (FLOT) and the plant-specific remorin (REM) protein families have been described as marker proteins for these membrane nanodomains (Raffaele et al, 2009; Jarsch and Ott, 2011; Li et al, 2012; Marin et al, 2012; Perraki et al, 2012; Hao et al, 2014; Jarsch et al, 2014; Wang et al, 2015; Bucherl et al, 2017; Gronnier et al, 2017; Liang et al, 2018) (Figure 1). This allowed comparative studies that revealed the co-existence of multiple nanodomains within the same cell (Jarsch et al, 2014). Similar concerns have been raised for the FLS2 co-receptor BAK1 (Ntoukakis et al, 2011)
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