Protein and lipid components in biological membranes act as a dynamic network of subtle molecular interactions segregating the membrane into particular highly dynamic regions called nanodomains. Nanodomains constitute functional platforms enriched in specific lipids (such as sterols and phosphoinositides) and proteins to perform their diverse activities. Remorins (REMs) are plant proteins and well-established nanodomain markers and can, as such, be considered as paradigm to provide a mechanistic description of membrane organisation into functional nanodomains. In a divide-and-conquer approach, we describe the impact of StREM1.3’s C-terminal membrane anchor (1), its oligomerization domain (2) and the intrinsically disordered region on membrane structure and dynamics. Furthermore, we tackle the structural features of StREM1.3 and its domains when associated to nanodomain-mimicking membranes by solid-state NMR. We show that StREM1.3 drives nanodomain organisation by concerted lipid-protein and protein-protein interactions, highlighting the dedicated role of each domain. We reveal a delicate balance between hydrophobic and electrostatic effects leading up to the protein’s characteristic affinity for negatively charged phospholipids.
(1) Gronnier J, et al.; Elife. 2017; 6. pii: e26404
(2) Martinez D, et al.; J Struct Biol. 2019; 206(1); 12-19