| Differential SNARE chaperoning by Munc13-1 and Munc18-1 dictates fusion pore fate at the release site. | Differential SNARE chaperoning by Munc13-1 and Munc18-1 dictates fusion pore fate at the release site.
Bhaskar BR, Yadav L, Sriram M, Sanghrajka K, Gupta M, V BK, Nellikka RK, Das D., Free PMC Article | 08/14/2024 |
| Vesicle capture by membrane-bound Munc13-1 requires self-assembly into discrete clusters. | Vesicle capture by membrane-bound Munc13-1 requires self-assembly into discrete clusters.
Li F, Kalyana Sundaram RV, Gatta AT, Coleman J, Ramakrishnan S, Krishnakumar SS, Pincet F, Rothman JE. | 10/2/2021 |
| Synaptotagmin-1-, Munc18-1-, and Munc13-1-dependent liposome fusion with a few neuronal SNAREs. | Synaptotagmin-1-, Munc18-1-, and Munc13-1-dependent liposome fusion with a few neuronal SNAREs.
Stepien KP, Rizo J., Free PMC Article | 06/12/2021 |
| Munc13 activates the Munc18-1/syntaxin-1 complex and enables Munc18-1 to prime SNARE assembly. | Munc13 activates the Munc18-1/syntaxin-1 complex and enables Munc18-1 to prime SNARE assembly.
Wang X, Gong J, Zhu L, Wang S, Yang X, Xu Y, Yang X, Ma C., Free PMC Article | 04/13/2021 |
| Re-examining how Munc13-1 facilitates opening of syntaxin-1. | Re-examining how Munc13-1 facilitates opening of syntaxin-1.
Magdziarek M, Bolembach AA, Stepien KP, Quade B, Liu X, Rizo J., Free PMC Article | 02/27/2021 |
| This study showed that the presynaptic terminal, Munc13-1 molecules form multiple and discrete supramolecular self-assemblies that serve as independent vesicular release sites by recruiting syntaxin-1 essential for synaptic vesicle exocytosis. | Synaptic weight set by Munc13-1 supramolecular assemblies.
Sakamoto H, Ariyoshi T, Kimpara N, Sugao K, Taiko I, Takikawa K, Asanuma D, Namiki S, Hirose K. | 05/11/2019 |
| Study data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly. | Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly.
Wang S, Li Y, Gong J, Ye S, Yang X, Zhang R, Ma C., Free PMC Article | 02/23/2019 |
| 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. | Inhibitory role of Munc13-1 in antigen-induced mast cell degranulation.
Higashio H, Satoh YI, Saino T. | 07/21/2018 |
| 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. | Critical Role of Trp-588 of Presynaptic Munc13-1 for Ligand Binding and Membrane Translocation.
Das J, Kedei N, Kelsey JS, You Y, Pany S, Mitchell GA, Lewin NE, Blumberg PM., Free PMC Article | 06/2/2018 |
| 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. | Autoinhibition of Munc18-1 modulates synaptobrevin binding and helps to enable Munc13-dependent regulation of membrane fusion.
Sitarska E, Xu J, Park S, Liu X, Quade B, Stepien K, Sugita K, Brautigam CA, Sugita S, Rizo J., Free PMC Article | 02/24/2018 |
| 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. | Mechanistic insights into neurotransmitter release and presynaptic plasticity from the crystal structure of Munc13-1 C(1)C(2)BMUN.
Xu J, Camacho M, Xu Y, Esser V, Liu X, Trimbuch T, Pan YZ, Ma C, Tomchick DR, Rosenmund C, Rizo J., Free PMC Article | 02/10/2018 |
| Overall, these results support a model whereby the multiple domains of Munc13 cooperate to coordinate synaptic vesicle docking, priming and fusion. | Functional synergy between the Munc13 C-terminal C1 and C2 domains.
Liu X, Seven AB, Camacho M, Esser V, Xu J, Trimbuch T, Quade B, Su L, Ma C, Rosenmund C, Rizo J., Free PMC Article | 10/7/2017 |
| 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. | Conformational change of syntaxin linker region induced by Munc13s initiates SNARE complex formation in synaptic exocytosis.
Wang S, Choi UB, Gong J, Yang X, Li Y, Wang AL, Yang X, Brunger AT, Ma C., Free PMC Article | 07/15/2017 |
| 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. | Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming.
Yang X, Wang S, Sheng Y, Zhang M, Zou W, Wu L, Kang L, Rizo J, Zhang R, Xu T, Ma C., Free PMC Article | 10/3/2015 |
| CAPS1 binds to the full-length of cytoplasmic syntaxin-1 with preference to its "open" conformation, whereas Munc13-1 binds to the first 80 N-terminal residues of syntaxin-1. | Calcium-dependent activator protein for secretion 1 (CAPS1) binds to syntaxin-1 in a distinct mode from Munc13-1.
Parsaud L, Li L, Jung CH, Park S, Saw NM, Park S, Kim MY, Sugita S., Free PMC Article | 11/2/2013 |
| 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+) | Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release.
Ma C, Su L, Seven AB, Xu Y, Rizo J., Free PMC Article | 02/9/2013 |
| the Rab3A cycle is coupled with the activation of Munc13-1 via RIM, which accounts for the regulation of secretion by Rab3A. | Involvement of Rab3A in vesicle priming during exocytosis: interaction with Munc13-1 and Munc18-1.
Huang CC, Yang DM, Lin CC, Kao LS. | 02/11/2012 |
| The C-terminal module of Munc13-1 is important for Munc13 function, but full activity requires adjacent modules. | The crystal structure of a Munc13 C-terminal module exhibits a remarkable similarity to vesicle tethering factors.
Li W, Ma C, Guan R, Xu Y, Tomchick DR, Rizo J., Free PMC Article | 02/11/2012 |
| The results show that Munc13 homology domain-1 is a SNARE-binding domain and that SNARE protein binding is essential for CAPS function in dense-core vesicle exocytosis. | Munc13 homology domain-1 in CAPS/UNC31 mediates SNARE binding required for priming vesicle exocytosis.
Khodthong C, Kabachinski G, James DJ, Martin TF., Free PMC Article | 01/7/2012 |
| Data show that Bassoon colocalizes with Aczonin at conventional synapses, but in ribbon synapses, CAST, Munc13, and RIM are segregated from Aczonin, and Aczonin is positioned and may control the access of neurotransmitter vesicles to the fusion site. | Molecular in situ topology of Aczonin/Piccolo and associated proteins at the mammalian neurotransmitter release site.
Limbach C, Laue MM, Wang X, Hu B, Thiede N, Hultqvist G, Kilimann MW., Free PMC Article | 10/29/2011 |
| The Munc13-1 MUN domain markedly accelerates the transition from the syntaxin-1-Munc18-1 complex to the SNARE complex. | Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex.
Ma C, Li W, Xu Y, Rizo J., Free PMC Article | 07/9/2011 |
| metabotropic glutamate receptor mGlu7 activates phospholipase C, translocates munc-13-1 protein, and potentiates glutamate release at cerebrocortical nerve terminals | The metabotropic glutamate receptor mGlu7 activates phospholipase C, translocates munc-13-1 protein, and potentiates glutamate release at cerebrocortical nerve terminals.
Martín R, Durroux T, Ciruela F, Torres M, Pin JP, Sánchez-Prieto J., Free PMC Article | 06/28/2010 |
| 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. | Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis.
Shin OH, Lu J, Rhee JS, Tomchick DR, Pang ZP, Wojcik SM, Camacho-Perez M, Brose N, Machius M, Rizo J, Rosenmund C, Südhof TC., Free PMC Article | 05/31/2010 |
| Presynaptic silencing was accompanied by decreases in levels of the priming proteins Munc13-1 and Rim1. | A role for the ubiquitin-proteasome system in activity-dependent presynaptic silencing.
Jiang X, Litkowski PE, Taylor AA, Lin Y, Snider BJ, Moulder KL., Free PMC Article | 03/8/2010 |
| 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. | Characterization of Munc13-1 and insulin secretion during pancreatic development in rats.
Yuan QX, Teng LP, Zhou JY, Liu CP, Guo J, Liu LJ, De W, Liu C. | 01/21/2010 |