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Chaperoning SNARE Folding and Assembly
Yongli Zhang1, Frederick M Hughson2
1Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520, USA;
Annual Review of Biochemistry
|April 7, 2021
Summary
Sec1/Munc18 (SM) proteins act as essential chaperones, facilitating the rapid and accurate assembly of SNARE proteins, which are crucial for intracellular membrane fusion and exocytosis. This review highlights recent biochemical and biophysical insights into the SNARE-SM fusion machinery.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- SNARE and Sec1/Munc18 (SM) proteins are central to intracellular membrane fusion and exocytosis.
- The precise physiological pathways of SNARE assembly and the mechanistic roles of SM proteins remain incompletely understood.
Purpose of the Study:
- To review recent advances in understanding the SNARE-SM fusion machinery, focusing on synaptic vesicle fusion.
- To elucidate the roles of SM proteins in SNARE assembly and membrane fusion.
Main Methods:
- Biochemical and biophysical studies of SNARE and SM proteins.
- In vitro analysis of SNARE folding, assembly, energetics, pathways, and kinetics.
- Investigation of SM-SNARE interactions and their in vivo impact.
Main Results:
- SM proteins function as chaperones, essential for enabling fast and accurate SNARE assembly.
- Evidence supports SM proteins collaborating with other SNARE chaperones like Munc13-1.
Conclusions:
- SM proteins are critical for efficient SNARE assembly, impacting membrane fusion and exocytosis.
- Deficiencies in SNARE and SM proteins are implicated in human diseases.
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