Genetic, proteomic, and structural analyses provide insight into the role of Brl1 during nuclear pore complex biogenesis, suggesting a function in the fusion of outer and inner nuclear membranes.

An interaction between the brown fat protein CIDEA and the phospholipid phosphatidic acid is vital for the expansion of intracellular lipid droplets for energy storage.

The amphipathic helix of perilipin 4 relies on the organization of its polar residues to form a remarkably immobile and stable protein layer on the surface of lipid droplets.

Membrane recruitment of BBSome is coupled to a conformational change, and interaction of the BBSome with GPCR cargoes depends on the GPCRs releasing their amphipathic helix 8 from the membrane.

A new structure reveals two Arf-GEF regulatory domains form a single structural unit that stimulates Arf-GEF activity.

A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.

Structures of the signal recognition particle before and after it captures a transmembrane domain suggest how it chooses, engages, and shields its clients during membrane protein targeting to the endoplasmic reticulum.

Structural comparison and electrophysiology of OSCA channels shed light on potential structural features influencing response to poke stimulus.

A disease-associated polymorphism in a related protein that regulates neurotransmitter release reveals that antiviral protein IFITM3 forms oligomers to rigidify membranes and inhibit virus fusion with cells.

The amphipathic helix at the C-terminus of Complexin II prevents premature secretion, whereas its N-terminal domain regulates mechanisms which are governed by the forward rate of Ca²⁺ binding to Synaptotagmin I.