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Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly
Shen Wang1, Yun Li1, Jihong Gong1
1Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology, 430074, Wuhan, China.
Nature Communications
|January 10, 2019
Summary
Munc13-1 facilitates exocytosis by interacting with synaptobrevin-2, enabling SNARE complex assembly. This interaction is crucial for vesicle recruitment and the transition to the final SNARE complex, orchestrated by Munc18-1 and Munc13-1.
Area of Science:
- Cellular Biology
- Neuroscience
- Biochemistry
Background:
- Exocytosis, the process of vesicle fusion with the plasma membrane, is critical for neurotransmission and hormone release.
- The formation of the SNARE complex, involving proteins like Munc18-1, syntaxin-1, SNAP-25, and synaptobrevin-2, is a key regulatory step in exocytosis.
- The precise mechanism by which Munc13-1 regulates the transition to the SNARE complex remains incompletely understood.
Purpose of the Study:
- To elucidate the molecular mechanism by which Munc13-1 regulates the transition of the Munc18-1/syntaxin-1 complex to the SNARE complex during exocytosis.
- To identify the specific interaction between Munc13-1 and synaptobrevin-2 that facilitates SNARE complex formation.
- To understand the sequential steps involving Munc13-1, Munc18-1, syntaxin-1, SNAP-25, and synaptobrevin-2 in orchestrating exocytosis.
Main Methods:
- Biochemical assays to identify protein-protein interactions.
- In vitro reconstitution of SNARE complex assembly.
- Analysis of vesicle recruitment and fusion dynamics.
Main Results:
- An essential interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2 was identified.
- Munc13-1 was shown to recruit synaptobrevin-2-containing vesicles to the target membrane.
- Munc13-1 enhances the accessibility of the synaptobrevin-2 SNARE motif for the Munc18-1/syntaxin-1 complex, facilitating subsequent SNAP-25 incorporation and SNARE complex completion.
Conclusions:
- Munc13-1 plays a pivotal role in regulating SNARE complex assembly by interacting with synaptobrevin-2.
- This interaction promotes vesicle docking and primes synaptobrevin-2 for SNARE complex formation, leading to efficient exocytosis.
- Munc18-1 and Munc13-1 function together as a template to orchestrate the sequential assembly of the SNARE complex for regulated exocytosis.
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