The structure, function and mechanism of the malaria vaccine candidate CelTOS reveal a unique pore-forming and membrane-disrupting protein with specificity for the inner leaflet of host and vector cells.
A structure of the complete, membrane bound, COPII coat solved by sub-tomogram averaging reveals the arrangement of all protein subunits on the membrane and suggests a mechanism for coating heterogeneously-shaped carriers.
The asymmetric combination of saturated and polyunsaturated acyl chains in phospholipids as typically observed in synapses makes membranes prone to deformation and fission without compromising their impermeability.
Unprecedented resolution of the molecular mechanisms of plant membrane protein anchoring involving phospholipids and sterols reveals the control of spatio-temporal segregation into plasma membrane nanodomains.
Computation and experiment together demonstrate that nonspecific membrane–protein interactions could regulate transmembrane protein function and suggest that covalent linkers can be an integral component of the sensing apparatus.