In vitro reconstitution shows how HIV-1 Gag assemblies on membranes can package the RNA genome in the presence of a vast excess of competing cellular RNAs, and that selectivity and immature lattice assembly are deeply intertwined with one another.

Advanced data analysis of molecular dynamics simulations of complex lipid membranes provides a quantitative and predictive model of the molecular features that control electroporation.

Spontaneous osmoregulation in giant phospholipid vesicles, which is characterized by oscillations in vesicle size and membrane tension, couples to the compositional degrees of freedom at the membrane surface to produce oscillations in domain texture and induce isothermal phase change.

Plasma membrane clusters of the Parkinson's disease protein α-synuclein colocalize with negatively charged phospholipids involved in endocytosis and exocytosis.

Hydrogen-deuterium exchange, electron microscopy, and vesicle reconstitution show how binding of the autophagy adaptor NDP52 to the FIP200 subunit of the ULK1 complex triggers membrane binding in autophagy.

The formation of HIV-1 particles requires a bending of the membrane that cannot be achieved by the Gag protein alone and thus there is need for the I-BAR protein IRSp53 to aid in the formation of HIV-1 buds.

Cooperative action of synaptotagmin and complexin is needed to arrest all SNARE complexes on a vesicle, and the reversal of the synaptotagmin clamp is sufficient to achieve fast, Ca²⁺-synchronized fusion.

Interactions were visualized between the nuclear egress complex from herpes simplex virus and a capsid protein that could promote nucleocytoplasmic translocation of the capsid in infected cells.

Complexin, in conjunction with Synaptotagmin, clamps the SNARE-assembly process under resting conditions and promote vesicle fusion in response to calcium signal.

Nanoscaleimaging reveals that animal septins form dense filamentous networks on biomimeticlipid membranes, explaining how septins may regulate cell surface rigidity.