Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming
Copyright policy )Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming
UNC-13-Munc13s have a central function in synaptic-vesicle priming through their MUN domains. However, it is unclear whether this function arises from the ability of the MUN domain to mediate the transition from the Munc18-1-closed syntaxin-1 complex to the SNARE complex in vitro. The crystal structure of the rat Munc13-1 MUN domain now reveals an elongated, arch-shaped architecture formed by α-helical bundles, with a highly conserved hydrophobic pocket in the middle. Mutation of two residues (NF) in this pocket abolishes the stimulation caused by the Munc13-1 MUN domain on SNARE-complex assembly and on SNARE-dependent proteoliposome fusion in vitro. Moreover, the same mutation in UNC-13 abrogates synaptic-vesicle priming in Caenorhabditis elegans neuromuscular junctions. These results support the notion that orchestration of syntaxin-1 opening and SNARE-complex assembly underlies the central role of UNC-13-Munc13s in synaptic-vesicle priming.
- Zhejiang Ocean University China (People's Republic of)
- Center for Excellence in Molecular Cell Science China (People's Republic of)
- Chinese Academy of Sciences China (People's Republic of)
- Huazhong University of Science and Technology China (People's Republic of)
- University of Chinese Academy of Sciences China (People's Republic of)
Models, Molecular, Molecular Sequence Data, Syntaxin 1, Nerve Tissue Proteins, Crystallography, X-Ray, Protein Structure, Tertiary, Rats, Mutation, Animals, Humans, Amino Acid Sequence, Synaptic Vesicles, Caenorhabditis elegans, SNARE Proteins
Models, Molecular, Molecular Sequence Data, Syntaxin 1, Nerve Tissue Proteins, Crystallography, X-Ray, Protein Structure, Tertiary, Rats, Mutation, Animals, Humans, Amino Acid Sequence, Synaptic Vesicles, Caenorhabditis elegans, SNARE Proteins
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