Protein and lipid components in biological membranes act as a dynamic network of subtle molecular inter-actions segregating the membrane into particular regions called nanodomains. Nanodomains act as func-tional platforms enriched in specific lipids (such as sterols and phosphoinositides) and proteins to performtheir diverse activities. Remorins (REMs) are plant proteins and well-established nanodomain markers and,as such, they can be considered as paradigm to provide a mechanistic description of membrane organisationinto functional nanodomains. Using solid-state nuclear magnetic resonance (ssNMR) and building upon ourinitial knowledge ofStREM1.3 and its C-terminal membrane anchor, we reveal the delicate balance betweenhydrophobic and electrostatic effects leading up to the protein’s characteristic affinity for negatively chargedphospholipids. In a divide-and-conquer approach, we describe the impact ofStREM1.3’s C-terminal anchor, itsoligomerisation domain and intrinsically disordered region on membrane structure and dynamics. Further-more, we tackle the structural features ofStREM1.3 when associated to nanodomain-mimicking membranes.We reveal thatStREM1.3 drives nanodomain organisation by concerted lipid-protein and protein-protein inter-actionsRead less <