Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly

• Published in: Nature communications Vol. 10; no. 1; pp. 69 - 14
• Main Authors: Wang, Shen, Li, Yun, Gong, Jihong, Ye, Sheng, Yang, Xiaofei, Zhang, Rongguang, Ma, Cong
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 08.01.2019; Nature Publishing Group; Nature Portfolio
• Subjects: 631/378/548/2589; 631/535/1266; 631/80/313/2104; 82/80; 82/83; 9/74; Animals; Assembly; BASIC BIOLOGICAL SCIENCES; Biophysics; Complex formation; Exocytosis; Gene Knockdown Techniques; HEK293 Cells; Humanities and Social Sciences; Humans; Laboratories; Membrane vesicles; Mice; multidisciplinary; Munc18 Proteins - metabolism; Mutation; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - metabolism; Neurons; Primary Cell Culture; Protein Binding - physiology; Protein Domains - physiology; Proteins; Science; Science (multidisciplinary); SNAP receptors; SNAP-25 protein; SNARE; Synaptic vesicle exocytosis; Synaptobrevin; Synaptosomal-Associated Protein 25 - metabolism; Syntaxin; Syntaxin 1; Syntaxin 1 - metabolism; Vesicle-Associated Membrane Protein 2 - metabolism; X-ray crystallography

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...