Dataset Information
Electron cryomicroscopy of NSF, the binary SNARE complex of SNAP-25 and syntaxin-1a, and alpha-SNAP under non-hydrolyzing conditions
Ontology highlight
ABSTRACT:
SUBMITTER: Kristopher Ian White
PROVIDER: EMPIAR-13136 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission.
Nature communications 20250924 1
Synaptic vesicles containing neurotransmitters fuse with the plasma membrane upon the arrival of an action potential at the active zone. Multiple proteins organize trans-SNARE complex assembly and priming, leading to fusion. One target membrane SNARE, syntaxin, forms nanodomains at the active zone, and another, SNAP-25, enters non-fusogenic complexes with it. Here, we reveal mechanistic details of AAA+ protein NSF (N-ethylmaleimide sensitive factor) and SNAP (soluble NSF attachment protein) acti ...[more]