6mdm
The 20S supercomplex engaging the SNAP-25 N-terminus (class 1)The 20S supercomplex engaging the SNAP-25 N-terminus (class 1)
Structural highlights
Function[VAMP2_RAT] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). [NSF_CRIGR] Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seem to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling. [STX1A_RAT] Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. [SNP25_RAT] t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. [SNAA_RAT] Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. Publication Abstract from PubMedThe recycling of SNARE proteins following complex formation and membrane fusion is an essential process in eukaryotic trafficking. A highly conserved AAA+ protein, NSF (N-ethylmaleimide sensitive factor) and an adaptor protein, SNAP (soluble NSF attachment protein), disassembles the SNARE complex. We report electron-cryomicroscopy structures of the complex of NSF, alphaSNAP, and the full-length soluble neuronal SNARE complex (composed of syntaxin-1A, synaptobrevin-2, SNAP-25A) in the presence of ATP under non-hydrolyzing conditions at ~3.9 A resolution. These structures reveal electrostatic interactions by which two alphaSNAP molecules interface with a specific surface of the SNARE complex. This interaction positions the SNAREs such that the 15 N-terminal residues of SNAP-25A are loaded into the D1 ring pore of NSF via a spiral pattern of interactions between a conserved tyrosine NSF residue and SNAP-25A backbone atoms. This loading process likely precedes ATP hydrolysis. Subsequent ATP hydrolysis then drives complete disassembly. Structural principles of SNARE complex recognition by the AAA+ protein NSF.,White KI, Zhao M, Choi UB, Pfuetzner RA, Brunger AT Elife. 2018 Sep 10;7. pii: 38888. doi: 10.7554/eLife.38888. PMID:30198481[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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