SummaryUnc13/Munc13s play a crucial function in neurotransmitter release through their MUN domain, which mediates the transition from the Syntaxin-1/Munc18-1 complex to the SNARE complex. The MUN domain was suggested to be related to tethering factors, but no MUN-domain structure is available to experimentally validate this notion and address key unresolved questions about the interactions and minimal structural unit required for Unc13/Munc13 function. Here we identify an autonomously folded module within the MUN domain (MUN-CD) and show that its crystal structure is remarkably similar to several tethering factors. We also show that the activity in promoting the Syntaxin-1/Munc18-1 to SNARE complex transition is strongly impaired in MUN-CD....
C(2) domains are well characterized as Ca(2+)/phospholipid-binding modules, but little is known abou...
P>Munc18-1 plays essential roles in neurosecretion by interacting with syntaxin-1 and controlling th...
Sec1/Munc18 (SM) family proteins are essential for every vesicle fusion pathway. The best-characteri...
SummaryUnc13/Munc13s play a crucial function in neurotransmitter release through their MUN domain, w...
The structure of the MUN domain of the synaptic protein Munc13-1 by Li et al., in this issue of Stru...
Abstract Neurotransmitter release requires SNARE complexes to bring membranes together, NSF-SNAPs to...
Munc18-1 and Syntaxin1 are essential proteins for SNARE-mediated neurotransmission. Munc18-1 partici...
Munc 18-1 and syntaxin-1A control SNARE-dependent neuroexocytosis and are organized in nanodomains o...
Exocytosis refers to a cellular process in which an intracellular vesicle fuses its membrane with th...
Munc18-1 plays a dual role in transporting syntaxin-1A (Sx1a) to the plasma membrane and regulating ...
Most nerve cells communicate with each other through synaptic transmission at chemical synapses. The...
The membrane fusion necessary for vesicle trafficking is driven by the assembly of heterologous SNAR...
The presynaptic active zone protein Munc13 is essential for neurotransmitter release, playing key ro...
Munc18-1 is essential for vesicle fusion and participates in the docking of large dense-core vesicle...
The membrane fusion necessary for vesicle trafficking is driven by the assembly of heterologous SNAR...
C(2) domains are well characterized as Ca(2+)/phospholipid-binding modules, but little is known abou...
P>Munc18-1 plays essential roles in neurosecretion by interacting with syntaxin-1 and controlling th...
Sec1/Munc18 (SM) family proteins are essential for every vesicle fusion pathway. The best-characteri...
SummaryUnc13/Munc13s play a crucial function in neurotransmitter release through their MUN domain, w...
The structure of the MUN domain of the synaptic protein Munc13-1 by Li et al., in this issue of Stru...
Abstract Neurotransmitter release requires SNARE complexes to bring membranes together, NSF-SNAPs to...
Munc18-1 and Syntaxin1 are essential proteins for SNARE-mediated neurotransmission. Munc18-1 partici...
Munc 18-1 and syntaxin-1A control SNARE-dependent neuroexocytosis and are organized in nanodomains o...
Exocytosis refers to a cellular process in which an intracellular vesicle fuses its membrane with th...
Munc18-1 plays a dual role in transporting syntaxin-1A (Sx1a) to the plasma membrane and regulating ...
Most nerve cells communicate with each other through synaptic transmission at chemical synapses. The...
The membrane fusion necessary for vesicle trafficking is driven by the assembly of heterologous SNAR...
The presynaptic active zone protein Munc13 is essential for neurotransmitter release, playing key ro...
Munc18-1 is essential for vesicle fusion and participates in the docking of large dense-core vesicle...
The membrane fusion necessary for vesicle trafficking is driven by the assembly of heterologous SNAR...
C(2) domains are well characterized as Ca(2+)/phospholipid-binding modules, but little is known abou...
P>Munc18-1 plays essential roles in neurosecretion by interacting with syntaxin-1 and controlling th...
Sec1/Munc18 (SM) family proteins are essential for every vesicle fusion pathway. The best-characteri...