Unc13a Antibody

1. These results suggested that Munc13-1 has an inhibitory role in antigen-induced mast cell degranulation, which is performed in a Munc13-4-dependent manner. PMID: 29225210
2. W22A, W22K, W22D, W22Y, and W22F substitutions were made in Munc13-1. The GFP-tagged constructs were expressed in Neuro-2a cells. Their membrane translocation in response to phorbol ester was observed in live cells by confocal microscopy. Munc13-1 translocated to the plasma membrane, the C1 domain translocated to internal membranes in response to phorbol ester. Trp-588 is important for ligand binding and translocation. PMID: 29244485
3. The structure imposes key constraints for models of neurotransmitter release and suggests that Munc13-1 bridges the vesicle and plasma membranes from the periphery of the membrane-membrane interface. PMID: 28177287
4. Overall, these results support a model whereby the multiple domains of Munc13 cooperate to coordinate synaptic vesicle docking, priming and fusion. PMID: 27213521
5. 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. PMID: 28137749
6. The crystal structure of the rat Munc13-1 MUN domain now reveals an elongated, arch-shaped architecture formed by alpha-helical bundles, with a highly conserved hydrophobic pocket in the middle. PMID: 26030875
7. The C-terminal module of Munc13-1 is important for Munc13 function, but full activity requires adjacent modules. PMID: 22000513
8. The Munc13-1 MUN domain markedly accelerates the transition from the syntaxin-1-Munc18-1 complex to the SNARE complex. PMID: 21499244
9. metabotropic glutamate receptor mGlu7 activates phospholipase C, translocates munc-13-1 protein, and potentiates glutamate release at cerebrocortical nerve terminals PMID: 20375012
10. Data suggest that, during repeated action potentials, Ca(2+) and phosphatidylinositolphosphate binding to the Munc13 C(2)B domain potentiate synaptic vesicle exocytosis, thereby offsetting synaptic depression induced by vesicle depletion. PMID: 20154707
11. Presynaptic silencing was accompanied by decreases in levels of the priming proteins Munc13-1 and Rim1. PMID: 20130189
12. Munc13-1 regulates insulin exocytosis PMID: 12871971
13. A conserved tryptophan residue occludes the diacylglycerol/phorbol ester-binding site in the munc13-1 C1 domain, and as a consequence, the munc13-1 C1 domain requires a considerable conformational change for ligand binding. PMID: 15667202
14. Study shows that the Munc13-1 C(2)A domain homodimerizes, and that homodimerization competes with Munc13-1/RIM heterodimerization. PMID: 16732694
15. Expression, purification and characterization of critical domains of Munc13-1 are reported. PMID: 17687497
16. Munc13s may provide a template to assemble syntaxin-1/SNAP-25 heterodimers, leading to an acceptor complex for synaptobrevin PMID: 18201107
17. These results suggest that Munc13-1 exists in pancreas islets during fetus development and its deficiency in the pancreas, as occurs in IUGR, was in accordance with decreased blood insulin level. PMID: 18787382

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KEGG: rno:64829

STRING: 10116.ENSRNOP00000025162

UniGene: Rn.10126