Stx1a cDNA ORF clone, Rattus norvegicus(Norway rat)

The Dual Function of the Polybasic Juxtamembrane Region of Syntaxin 1A in Clamping Spontaneous Release and Stimulating Ca
Singer-Lahat D, Barak-Broner N, Sheinin A, Greitzer-Antes D, Michaelevski I, Lotan I
The Journal of neuroscience : the official journal of the Society for Neuroscience38(1)220-231(2018 Jan)

The SNARE Protein Syntaxin-1a Plays an Essential Role in Biphasic Exocytosis of the Incretin Hormone Glucagon-Like Peptide 1.
Wheeler SE, Stacey HM, Nahaei Y, Hale SJ, Hardy AB, Reimann F, Gribble FM, Larraufie P, Gaisano HY, Brubaker PL
Diabetes66(9)2327-2338(2017 09)

G?? directly modulates vesicle fusion by competing with synaptotagmin for binding to neuronal SNARE proteins embedded in membranes.
Zurawski Z, Page B, Chicka MC, Brindley RL, Wells CA, Preininger AM, Hyde K, Gilbert JA, Cruz-Rodriguez O, Currie KPM, Chapman ER, Alford S, Hamm HE
The Journal of biological chemistry292(29)12165-12177(2017 07)

An activated Q-SNARE/SM protein complex as a possible intermediate in SNARE assembly.
Jakhanwal S, Lee CT, Urlaub H, Jahn R
The EMBO journal36(12)1788-1802(2017 06)

Data suggest that GTP-binding protein beta/gamma (Gb/g) heterodimers interact specifically with lipid-embedded neuronal t-SNARE proteins syntaxin 1A and SNAP-25B (synaptosomal-associated protein 25B); this binding is competitive with synaptotagmin 1 for binding sites on the t-SNARE proteins; Gb/g inhibits Ca2+/synaptotagmin 1-dependent membrane fusion.
Title: G?? directly modulates vesicle fusion by competing with synaptotagmin for binding to neuronal SNARE proteins embedded in membranes.

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.
Title: An activated Q-SNARE/SM protein complex as a possible intermediate in SNARE assembly.

Here, the authors identified two conserved residues (R151, I155) in the syntaxin-1 linker region as key sites for the Munc13-1 MUN domain interaction. This interaction is essential for SNARE complex formation in vitro and synaptic vesicle priming in neuronal cultures.
Title: Conformational change of syntaxin linker region induced by Munc13s initiates SNARE complex formation in synaptic exocytosis.

Our results suggest that, as in the CNS, CADM1 interactions drive exocytic site assembly and promote actin network formation. These results support the broader hypothesis that the effects of cell-cell contact on beta-cell maturation and function are mediated by the same extracellular protein interactions that drive the formation of the presynaptic exocytic machinery. These interactions may be therapeutic targets for re...
Title: Extracellular CADM1 interactions influence insulin secretion by rat and human islet ?-cells and promote clustering of syntaxin-1.

Ca(2+)acts as a charge bridge that specifically and reversibly connects multiple syntaxin 1/Phosphatidylinositol 4,5-Bisphosphate complexes into larger mesoscale domains.
Title: Calcium Promotes the Formation of Syntaxin 1 Mesoscale Domains through Phosphatidylinositol 4,5-Bisphosphate.