The C terminal fusion partners of TAZ-CAMTA1, YAP-TFE3 and potentially other TAZ/YAP fusion proteins in cancer recruit epigenetic modifiers that modulate a baseline TEAD-based transcriptional program.

During neurotransmitter release, calcium-induced membrane insertion of the C2B domain of Synaptotagmin re-orients the bound SNARE complex which dilates the fusion pore in a mechanical lever action.

A few SNARE complexes suffice to fuse membranes, but many more are needed to dilate the nascent fusion pore by molecular crowding for efficient neurotransmitter or hormone release during exocytosis.

A combination of advanced optical imaging and cryogenic electron microscopy has been used to explore membrane fusion in a synthetic system and provide new insights into neurotransmitter release.

Single-molecule localization imaging shows that the Nipah virus fusion protein forms nanoscale clusters on cell and viral membranes that favor membrane fusion activation.

The mechanism triggering HBV membrane fusion involves ERp57, a cellular protein disulfide isomerase, and ultimately leads to the exposition of a fusion peptide that was identified in the pre-S1 determinant.

Hantavirus spikes are related laterally by 2-fold Gc contacts that can be disulfide-linked and display a temperature-dependent dynamic behavior at neutral pH, exposing and masking the Gc fusion loops.

Structure, dynamics, and mutation of a gamete fusion protein and comparisons to viral homologues suggest that after trimerization the domain bearing the membrane-inserting fusion loops can pivot with respect to the trimer 3-fold axis.

The mechanism of membrane-fusion catalysis in influenza viral infection of target cells is robust against the presence of a large fraction of non-productive viral fusion proteins.

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.