Abstract
Nanodomains are dynamic membrane subcompartments, enriched in specific lipid, and protein components that act as functional platforms to manage an abundance of cellular processes. The remorin protein of plants is a well-established nanodomain marker and widely serves as a paradigm to study nanodomain clustering. Located at the inner leaflet of the plasma membrane, remorins perform essential functions during signaling. Using deuterium and phosphorus solid-state NMR, we inquire on the molecular determinants of the lipid-protein and protein-protein interactions driving nanodomain clustering. By monitoring thermotropism properties, lipid acyl chain order and membrane thickness, we report the effects of phosphoinositides and sterols on the interaction of various remorin peptides and protein constructs with the membrane. We probed several critical residues involved in this interaction and the involvement of the coiled-coil homo-oligomerisation domain into the formation of remorin nanodomains. We trace the essential role of the pH in nanodomain clustering based on anionic lipids such as phosphoinositides. Our results reveal a complex interplay between specific remorin residues and domains, the environmental pH and their resulting effects on the lipid dynamics for phosphoinositide-enriched membranes.
Highlights
The fluid mosaic model of Singer and Nicolson (1972) describes a biological membrane as a bilayer of phospholipids, hydrophobic parts buried and hydrophilic parts exposed, with membrane proteins spanning or anchoring to the bilayer
Using 2H ssNMR, we monitored thermotropism, lipid dynamics, and membrane thickness of liposomes containing consecutively the different membrane components that might impact on remorin-driven nanodomain assembly
We employed a 2H ssNMRbased methodology to tackle the lipid-protein interactions and mechanisms behind nanodomain clustering driven by StREM1.3
Summary
The fluid mosaic model of Singer and Nicolson (1972) describes a biological membrane as a bilayer of phospholipids, hydrophobic parts buried and hydrophilic parts exposed, with membrane proteins spanning or anchoring to the bilayer. In this model, lipid heterogeneity, and precise lipid-protein interactions that might lead to cooperative local enrichment of specific components, i.e., nanodomain organization becomes conceivable. Lipid heterogeneity, and precise lipid-protein interactions that might lead to cooperative local enrichment of specific components, i.e., nanodomain organization becomes conceivable Due to their eclectic composition, membranes are key players in cell biology, and have a plethora of functions (Grecco et al, 2011; Ott, 2017), constituting prime drug design targets. Considering typical nanodomain compositions, these membrane regions should have a tendency of manifesting Lo behavior, usually containing lipids fostering liquid order such as sterols
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