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Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association

by Jiao, Junyi , Xu, Yonggang , Hughson, Frederick M , Eisemann, Travis J , Wang, Yukun , He, Mengze , Xiong, Yujian , Port, Sarah A , Zhang, Yongli , Qu, Hong , Baker, Richard W , Jin, Huaizhou

in Catalysis / Cell Biology / Exocytosis / Membrane fusion / optical tweezers / Polypeptides / Proteins / Sec1/Munc18 (SM) proteins / Sm proteins / SNAP receptors / SNAP-25 protein / SNARE assembly / SNARE proteins / Software / Spectroscopy / Structural Biology and Molecular Biophysics / Syntaxin / template complex

2018

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Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association

by Jiao, Junyi , Xu, Yonggang , Hughson, Frederick M , Eisemann, Travis J , Wang, Yukun , He, Mengze , Xiong, Yujian , Port, Sarah A , Zhang, Yongli , Qu, Hong , Baker, Richard W , Jin, Huaizhou

2018

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Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association

by Jiao, Junyi , Xu, Yonggang , Hughson, Frederick M , Eisemann, Travis J , Wang, Yukun , He, Mengze , Xiong, Yujian , Port, Sarah A , Zhang, Yongli , Qu, Hong , Baker, Richard W , Jin, Huaizhou

2018

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Journal Article

Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association

Jiao, Junyi,

Xu, Yonggang,

Hughson, Frederick M,

Eisemann, Travis J,

Wang, Yukun,

He, Mengze,

Xiong, Yujian,

Port, Sarah A,

Zhang, Yongli,

Qu, Hong,

Baker, Richard W,

Jin, Huaizhou

2018

Overview

Sec1/Munc18-family (SM) proteins are required for SNARE-mediated membrane fusion, but their mechanism(s) of action remain controversial. Using single-molecule force spectroscopy, we found that the SM protein Munc18-1 catalyzes step-wise zippering of three synaptic SNAREs (syntaxin, VAMP2, and SNAP-25) into a four-helix bundle. Catalysis requires formation of an intermediate template complex in which Munc18-1 juxtaposes the N-terminal regions of the SNARE motifs of syntaxin and VAMP2, while keeping their C-terminal regions separated. SNAP-25 binds the templated SNAREs to induce full SNARE zippering. Munc18-1 mutations modulate the stability of the template complex in a manner consistent with their effects on membrane fusion, indicating that chaperoned SNARE assembly is essential for exocytosis. Two other SM proteins, Munc18-3 and Vps33, similarly chaperone SNARE assembly via a template complex, suggesting that SM protein mechanism is conserved.

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eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd

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