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Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission
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Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission
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Journal Article
Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission
2025
Overview
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) action before fusion. We show that syntaxin clusters are conserved, that NSF colocalizes with them, and characterize SNARE populations that may exist within or near them using cryo-EM. Supercomplexes of NSF, α-SNAP, and either a syntaxin tetramer or one of two binary complexes of syntaxin—SNAP-25 reveal atomic details of SNARE processing and show how sequential ATP hydrolysis drives disassembly. These results suggest a functional role for syntaxin clusters as reservoirs and a corresponding role for NSF in syntaxin liberation and SNARE protein quality control preceding fusion.
NSF hydrolyzes ATP to disassemble SNARE complexes. Here, the authors find NSF colocalizes with syntaxin nanodomains, reveal disassembly of syntaxin oligomers and other pre-fusion cis-SNARE complexes by NSF, and show how sequential hydrolysis drives disassembly.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/63
/ 82/16
/ 82/29
/ 82/80
/ 82/83
/ Adenosine Triphosphate - metabolism
/ Animals
/ Clusters
/ Humanities and Social Sciences
/ Humans
/ N-Ethylmaleimide-Sensitive Proteins - chemistry
/ N-Ethylmaleimide-Sensitive Proteins - metabolism
/ Plasma
/ Proteins
/ Qa-SNARE Proteins - chemistry
/ Qa-SNARE Proteins - metabolism
/ Rats
/ Science
/ Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - chemistry
/ Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - metabolism
/ Synaptic Transmission - physiology
/ Synaptic Vesicles - metabolism
/ Synaptosomal-Associated Protein 25 - chemistry
/ Synaptosomal-Associated Protein 25 - metabolism
/ Syntaxin
