Snapin: a SNARE–associated protein implicated in synaptic transmission

@article{Ilardi1999SnapinAS,
  title={Snapin: a SNARE–associated protein implicated in synaptic transmission},
  author={Jeffrey M. Ilardi and Sumiko Mochida and Zu-Hang Sheng},
  journal={Nature Neuroscience},
  year={1999},
  volume={2},
  pages={119-124}
}
Synaptic vesicle docking and fusion are mediated by the assembly of a stable SNARE core complex of proteins, which include the synaptic vesicle membrane protein VAMP/synaptobrevin and the plasmalemmal proteins syntaxin and SNAP–25. We have now identified another SNAP–25–binding protein, called Snapin. Snapin was enriched in neurons and exclusively located on synaptic vesicle membranes. It associated with the SNARE complex through direct interaction with SNAP–25. Binding of recombinant Snapin–CT… Expand
SNAP-29: A general SNARE protein that inhibits SNARE disassembly and is implicated in synaptic transmission
TLDR
It is suggested that SNAP-29 may function as a regulator of SNARE complex disassembly and modulate the process of postfusion recycling of the SNARE components. Expand
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TLDR
It is suggested that syntaphilin may function as a molecular clamp that controls free syntaxin-1 availability for the assembly of the SNARE complex, and thereby regulates synaptic vesicle exocytosis. Expand
Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells.
TLDR
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TLDR
It is proposed that the primary role of Snapin in C. elegans is to promote vesicle priming, consistent with the stabilization of SNARE complex formation through established interactions with SNAP-25 upstream of the actions of Synaptotagmin in calcium-sensing and endocytosis. Expand
Protein–protein interactions in neurotransmitter release
  • S. Mochida
  • Medicine, Biology
  • Neuroscience Research
  • 2000
TLDR
Functional studies in last half decade on synaptic-terminal proteins have revealed that the SNARE core complex, consisting of synaptobrevin VAMP, a synaptic vesicle-associated protein, syntaxin and SNAP-25, synaptic membrane-associated proteins, acts as the membrane fusion machinery. Expand
Calcium‐Dependent Dissociation of Synaptotagmin from Synaptic SNARE Complexes
TLDR
These findings are consistent with models in which the Ca2+‐triggered release of synaptotagmin precedes vesicle fusion, and suggest that constitutive SNARE complex disassembly occurs in undocked synaptic vesicles. Expand
Reinvestigation of the Role of Snapin in Neurotransmitter Release*
TLDR
It is concluded that the postulated role of snapin as a SNARE regulator in neurotransmitter release needs reconsideration, leaving the true function of this evolutionarily conserved protein to be discovered. Expand
Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex
TLDR
The results indicate that Snapin may be a PKA target for modulating transmitter release through the cAMP-dependent signal-transduction pathway. Expand
Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation.
TLDR
Results indicate that snapin plays a role in tethering insulin granules to the plasma membrane through coiled coil interaction of snapin with SNAP-25, with full granule fusion competency only resulting after subsequent syntaxin-1A recruitment triggered by secretory stimulation. Expand
Identification of a novel SNAP25 interacting protein (SIP30)
TLDR
A cDNA coding for a novel protein of 266 amino acids is identified that is named SIP30 (SNAP25 interacting protein of 30 kDa), which is expressed abundantly in brain and slightly in testis and kidney and may be indirectly associated with syntaxin, perhaps through SNAP25. Expand
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