6A30

Crystal Structure of Munc13-1 MUN Domain and Synaptobrevin-2 Juxtamembrane Linker Region

Summary for 6A30

• Entry DOI: 10.2210/pdb6a30/pdb
• Descriptor: Protein unc-13 homolog A, Synaptobrevin-2 juxtamembrane linker peptide (3 entities in total)
• Functional Keywords: synaptic exocytosis, membrane fusion, munc13, munc18, snare, synaptobrevin, exocytosis
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 2
• Total formula weight: 62726.85

Authors

Wang, S.,Li, Y.,Gong, J.H.,Ye, S.,Yang, X.F.,Zhang, R.G.,Ma, C. (deposition date: 2018-06-14, release date: 2019-01-30, Last modification date: 2023-11-22)

Primary citation

Wang, S.,Li, Y.,Gong, J.H.,Ye, S.,Yang, X.F.,Zhang, R.G.,Ma, C.
Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly.
Nat Commun, 10:69-69, 2019

PubMed Abstract: The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly.

PubMed: 30622273
DOI: 10.1038/s41467-018-08028-6

Experimental method

X-RAY DIFFRACTION (2.793 Å)