Recombinant Rat Syntaxin-binding protein 1 (Stxbp1)

1. Together with previous studies, these data support a model whereby Munc18-1 acts as a template for SNARE complex assembly, and autoinhibition of synaptobrevin binding contributes to enabling regulation of neurotransmitter release by Munc13-1. PMID: 28477408
2. Munc18a promotes membrane clustering in a step that is independent of trans-SNARE activation. PMID: 28827281
3. The ternary complex of syntaxin1:SNAP25:Munc18-1binds synaptobrevin with fast kinetics, resulting in the rapid formation of a fully zippered SNARE complex to which Munc18-1 remains tethered by the N-terminal domain of syntaxin1. PMID: 28483813
4. Munc18-1 mutations and haploinsufficiency may therefore trigger a pathogenic gain of function through both the corruption of native Munc18-1 and a perturbed chaperone activity for alpha-Syn leading to aggregation-induced neurodegeneration. PMID: 27597756
5. TNFalpha induces co-trafficking of TRPV1/TRPA1 in VAMP1-containing vesicles to the plasmalemma via Munc18-1/syntaxin1/SNAP-25 mediated fusion. PMID: 26888187
6. Data demonstrate that the open-closed syntaxin equilibrium is shifted toward the open state when syntaxin and Munc18-1 are associated with SNAP25, and the results indicate that a syntaxin/SNAP25:Munc18-1 complex is a likely starting point for SNARE assembly. PMID: 26876096
7. Measuring rapid interaction dynamics during synaptic depolarization identified the small number of syntaxin1a and munc18-1 protein molecules required to support synaptic vesicle exocytosis. PMID: 25517944
8. Secretory vesicles dock by inducing syntaxin1/munc18 clustering in the target membrane. PMID: 24835618
9. Munc18a does not alter synaptic fusion rates mediated by neuronal SNAREs, synaptotagmin-1, and complexin-1. PMID: 25716318
10. Synaptotagmin-1 is an antagonist for Munc18-1 in SNARE zippering. PMID: 25716321
11. SEC1/Munc18-SNARE interactions at other transport steps may provide a general mechanism to drive lipid bilayer merger. PMID: 24532794
12. PTPRT could regulate the interaction of Syntaxin-binding protein 1 with Syntaxin 1, and as a result, the synaptic vesicle fusion appears to be controlled through dephosphorylation of Syntaxin-binding protein 1 PMID: 23962429
13. the priming mechanism of Munc18-1 involves its domain-3a-dependent interaction with the SNARE complex. PMID: 23525015
14. a defined role for Munc18-1 in facilitating exocytosis linked to the loop region of domain 3a that is clearly distinct from its function in Sx1a transport. PMID: 23761923
15. Double knockdown of Munc18-1 and Munc18-2 in mast cells eliminates both IgE-dependent and ionomycin-induced degranulation and causes a significant reduction in syntaxin-11 without altering expressions of the other syntaxin isoforms examined. PMID: 23487749
16. Munc18-1 molecules move between membrane depots distinct from vesicle morphological docking sites PMID: 23223447
17. it is proposed that fusion does not proceed through syntaxin-1-SNAP-25 heterodimers but starts with the syntaxin-1-Munc18-1 complex; Munc18-1 and Munc13 then orchestrate membrane fusion together with the SNAREs and synaptotagmin-1-Ca(2+) PMID: 23258414
18. SNAREpin assembly by Munc18-1 requires previous vesicle docking by synaptotagmin 1. PMID: 22810233
19. Munc18 can control and assist in SNARE-complex assembly during neurotransmitter release PMID: 21900493
20. the domain-1 cleft of Munc18-1 is essential for binding to syntaxin-1 and thereby critical for its chaperoning, docking, and secretory functions PMID: 21900502
21. Munc18-1 acts downstream of Munc13-1/RIM/Rab3A and interacts with syntaxin 1a allowing vesicle priming. Munc18-1 promotes Rab3A dissociation from vesicles, which then results in fusion. PMID: 21689256
22. This suggests that Munc18a controls the accessibility of syntaxin 1a to its partners, a role that might be common to all Sec1/Munc18-like proteins. PMID: 18337752
23. Munc18-1 and the neuronal SNAREs (t-SNARE (syntaxin 1.SNAP-25) and v-/t-SNARE (VAMP2.syntaxin 1.SNAP-25) complexes) already have the inherent capability to function as a basic stage-specific off/on switch to control membrane fusion PMID: 21730064
24. results suggest that excitatory stimulation can induce the distribution change of Munc18-1 in neuron, which may subsequently modulate neuronal functions in brain. PMID: 21614099
25. Munc18-1 allows for the formation of a complex between syntaxin and SNAP-25 that serves as an acceptor for vesicle-bound synaptobrevin PMID: 17002520
26. The results of molecular dynamics simulations suggest that the free wild-type munc18a exhibits a dynamic equilibrium between several conformations differing in the size of its cavity (the main syntaxin-binding site). PMID: 21390273
27. Data show that a phosphorylation site in syntaxin 1 (Ser(14)) regulates the N-terminal interaction with Munc18-1. PMID: 19748891
28. Results indicate that Munc18-1 and -2 act to support the expression of syntaxins and to deliver syntaxin-1 to the plasma membrane, and that the binding to the closed conformation of syntaxin is essential for Munc18-1 stimulatory action. PMID: 19812250
29. Since Munc-18a can bind both isoforms of syntaxin 1, the present data suggest that this protein is a general modulator of the formation of different SNARE complexes in the nerve endings. PMID: 12093152
30. nSec1/Munc18a is involved in the regulation of SNARE complex-dependent membrane fusion events implicated in the ramification of axonal processes in hippocampal neurons. PMID: 12182895
31. the biochemical evidence of strong interaction between Munc18-1 with cytoskeletal proteins PMID: 12963086
32. Munc-18-1 is a potent negative regulator of basal phospholipase D activity PMID: 14744865
33. Syntaxin/Munc18 interactions in the late events during vesicle fusion and release in exocytosis PMID: 15175344
34. Munc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactions. PMID: 15563604
35. The presence of both nuclear import and export signals in Munc18-1 primary structure corroborates its nuclear localization and makes it a putative shuttle protein between nuclear and cytoplasmic compartments. PMID: 15869823
36. Munc18-1, expressed in an estrogen-dependent manner, plays an important role in the onset of female puberty via the regulation of glutamate release. PMID: 16951547
37. Munc18-1 accelerates fusion only for the cognate SNAREs for exocytosis, therefore enhancing fusion specificity. PMID: 17218264
38. Up-regulated ny estradiol. PMID: 17293448
39. Munc18-1 also binds tightly to assembled SNARE complexes containing syntaxin-1. PMID: 17301226
40. We propose that Munc18-1 inhibitis the SNARE complex assembly by stabilizing Syntaxin1A in a closed conformation in vesicle priming process, therefore negatively regulates insulin secretion. PMID: 17617378
41. Munc18-1 plays a critical role for the plasma membrane localization of syntaxin1 in neuroendocrine cells and therefore necessitates the interpretation of Munc18-1 mutant phenotypes to be in terms of mislocalized syntaxin1. PMID: 18077557
42. Data suggest that Munc18a binds to the Syntaxin1a NRD and H3 domain within the assembled t-SNARE complex, positioning them for productive VAMP2 binding, so that Munc18a facilitates efficient SNARE-mediated membrane fusion. PMID: 18829865
43. Immunohistochemical analysis revealed that the protein level of syntaxin1 was markedly up-regulated in the ischemic areas where immunoreaction for MAP2 was lost. PMID: 19344701
44. The Munc18-1 hydrophobic pocket is therefore critical for SNARE complex binding PMID: 19483085
45. In primary cultured hippocampal neurons, a role is suggested for schizophrenia-related dysbindin in synaptic vesicle exocytosis via interaction with Munc18-1. PMID: 19573021
46. show that presynaptic metabotropic glutamate receptors (mGluRs) bind and release Munc18-1 in a Ca(2+)-dependent manner, whose actions decrease and increase synaptic vesicle release, respectively. PMID: 19822743

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KEGG: rno:25558

STRING: 10116.ENSRNOP00000021189

UniGene: Rn.80843