The complex is tetrameric with two parallel syntaxins Analyses suggested the presence of two syntaxin components in the full-length syntaxin–SNAP-25 t-SNARE complex 5. Gel filtration analysis ...

We show here that SNARE complex binding of complexin I (CplxI) via its central α-helix is necessary but, unexpectedly, not sufficient for its key function in promoting neurotransmitter release.

Scientists now report that NSF/?-SNAP disassemble a single SNARE complex using various single-molecule biophysical methods that allow them to monitor and manipulate individual protein complexes.

SNARE proteins are a large protein superfamily consisting of more than 60 members in yeast and mammals. The primary role of these proteins is to mediate fusion of vesicles with their target membrane ...

The ATPase NSF (N-ethylmaleimide sensitive factor), together with SNAPs, disassembles the SNARE complex into its protein components, allowing for subsequent rounds of fusion.

By revealing the complex's X-ray crystal structure, however, this paper has helped scientists devise appropriate SNARE experiments that continue to elucidate the protein.

Autophagy, traditionally known for degrading and recycling cytoplasmic components to maintain cellular homeostasis, has recently emerged as a novel route for the unconventional secretion of ...