Specificity and regulation of a synaptic vesicle docking complex

@article{Pevsner1994SpecificityAR,
  title={Specificity and regulation of a synaptic vesicle docking complex},
  author={Jonathan Pevsner and S C Hsu and Janice E. A. Braun and Nicole Calakos and A E Ting and Mark K. Bennett and Richard H. Scheller},
  journal={Neuron},
  year={1994},
  volume={13},
  pages={353-361}
}
Synaptic vesicles are proposed to dock at the presynaptic plasma membrane through the interaction of two integral membrane proteins of synaptic vesicles, VAMP and synaptotagmin, and two plasma membrane proteins, syntaxin and SNAP-25. We have characterized the binding properties of these proteins and observed SNAP-25 potentiation of VAMP 2 binding to syntaxins 1a and 4 but not syntaxins 2 or 3. n-sec1, a neuron-specific syntaxin-binding protein, bound syntaxin with nanomolar affinity, forming a… Expand
Association of syntaxin with SNAP‐25 and VAMP (synaptobrevin) during axonal transport
TLDR
Heterotrimeric complexes containing syntaxin, SNAP‐25, and VAMP are already formed during fast anterograde axonal transport, before reaching the nerve endings. Expand
Distinct domains of syntaxin are required for synaptic vesicle fusion complex formation and dissociation
TLDR
It is demonstrated that unique, yet overlapping, domains of syntaxin are required to form these complexes, consistent with the hypothesis that conformational changes in syntaxin, resulting from protein-protein interactions and ATP hydrolysis by NSF, mediate neurotransmitter release. Expand
Effect of Mutations in Vesicle-Associated Membrane Protein (VAMP) on the Assembly of Multimeric Protein Complexes
TLDR
A correlation exists between the membrane-trafficking phenotype of the two VAMP-2 point mutants and their competence to form complexes with either syntaxin 1A or SNAP-25. Expand
Hrs-2 is an ATPase implicated in calcium-regulated secretion
TLDR
The results suggest a role for Hrs-2 in regulating secretory processes through calcium- and nucleotide-dependent modulation of vesicle-trafficking protein complexes through calcium's role in neurotransmitter-containing vesicles and on the presynaptic membrane. Expand
The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling
TLDR
It is demonstrated that major pools of syntaxin 1 and SNAP-25 recycle with SVs, concluding that t- SNAREs participate in SV recycling in what may be functionally distinct forms. Expand
Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses.
TLDR
This interaction appears to resolve the apparent paradox that synaptic vesicles are capable of docking even when VAMP (vesicle-associated membrane protein) or syntaxin is cleaved or deleted and suggests that two species of v-SNAREs (VAMP and synaptotagmin) and two species (SNAP-25 and syntaxin) interact to functionally dock synaptic vESicles. Expand
Structural Organization of the Synaptic Exocytosis Core Complex
TLDR
The data indicate that syntaxin and VAMP bind primarily in a parallel arrangement and suggest a coiled-coil structure that is bent rather than fully extended, and a model in which binding of SNAP receptor (SNARE) protein co- coils domains helps drive vesicle fusion. Expand
Identification of a Novel Syntaxin- and Synaptobrevin/VAMP-binding Protein, SNAP-23, Expressed in Non-neuronal Tissues*
TLDR
Using the yeast two-hybrid system, a 23-kDa protein from human B lymphocytes is identified that binds tightly to multiple syntaxins and synaptobrevins/VAMPs in vitro and suggests that SNAP-23 is an essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion in all mammalian cells. Expand
Synaptic Core Complex of Synaptobrevin, Syntaxin, and SNAP25 Forms High Affinity -SNAP Binding Site (*)
TLDR
Data suggest that the complex of the vesicular protein synaptobrevin with the plasma membrane protein syntaxin is required for physiological α-SNAP binding, which probably functions in a late step of the membrane fusion reaction after the formation of the synaptOBrevin-syntaxin- SNAP25 core complex. Expand
nSec 1 Binds a Closed Conformation of Syntaxin 1 A
The Sec1 family of proteins is proposed to function in vesicle trafficking by forming complexes with target membrane SNAREs (soluble N -ethylmaleimide-sensitive factor [NSF] attachment protein [SNAP]Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 28 REFERENCES
A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
TLDR
It is reported that in the absence of SNAP and NSF, these three SNAREs form a stable complex that can also bind synaptotagmin, suggesting that synapttagmin operates as a "clamp" to prevent fusion from proceeding in the absent of a signal. Expand
Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
TLDR
The discovery of a brain protein of relative molecular mass 67,000 (67K) which binds stably to syntaxin suggests that Munc-18 is a previously unidentified essential component of the synaptic vesicle fusion protein complex. Expand
Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones.
TLDR
Two 35-kilodalton proteins (p35 or syntaxins) were identified that interact with the synaptic vesicle protein p65 (synaptotagmin) and may function in docking synaptic vESicles near calcium channels at presynaptic active zones. Expand
The syntaxin family of vesicular transport receptors
TLDR
Results indicate that the syntaxins are a family of receptors for intracellular transport vesicles and that each target membrane may be identified by a specific member of the syntaxin family. Expand
SNAP receptors implicated in vesicle targeting and fusion
TLDR
The existence of numerous SNARE-related proteins, each apparently specific for a single kind of vesicles or target membrane, indicates that NSF and SNAPs may be universal components of a vesicle fusion apparatus common to both constitutive and regulated fusion (including neurotransmitter release), in which the SNAREs may help to ensure vesICLE-to-target specificity. Expand
n-Sec1: a neural-specific syntaxin-binding protein.
TLDR
Findings indicate that n-Sec1 is a neural-specific, syntaxin-binding protein that may participate in the regulation of synaptic vesicle docking and fusion. Expand
Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking.
TLDR
A physical basis for the specificity of intracellular vesicle transport is suggested by the demonstration of specific interaction between vesicular proteins and plasma membrane proteins. Expand
Synaptic vesicle membrane proteins interact to form a multimeric complex
TLDR
The protein interactions defined in this report are likely to underlie aspects of neurotransmitter secretion, membrane traffic, and the spatial organization of vesicles within the nerve terminal. Expand
SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast
TLDR
Data suggest that the mechanism of action of SNAPs in membrane fusion is conserved in evolution, and may be an early stage in the assembly of a proposed multisubunit "fusion machine" on the target membrane. Expand
Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein
TLDR
The results suggest that constitutive and regulated vesicular pathways use homologous proteins for membrane trafficking, probably for membrane fusion at the plasma membrane, indicating a greater mechanistic and evolutionary similarity between these pathways than previously thought. Expand
...
1
2
3
...