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Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion

Author

Listed:
  • Peng Yue

    (University of Pennsylvania)

  • Yubo Zhang

    (Max F. Perutz Laboratories, Medical University of Vienna
    Present address: School of Materials Science and Energy Engineering, Foshan University, Foshan, Guangdong Province 528000, China)

  • Kunrong Mei

    (University of Pennsylvania)

  • Shaoxiao Wang

    (University of Pennsylvania)

  • Johannes Lesigang

    (Max F. Perutz Laboratories, Medical University of Vienna)

  • Yueyao Zhu

    (University of Pennsylvania)

  • Gang Dong

    (Max F. Perutz Laboratories, Medical University of Vienna)

  • Wei Guo

    (University of Pennsylvania)

Abstract

The soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (SNAREs) constitute the core machinery for membrane fusion during eukaryotic cell vesicular trafficking. However, how the assembly of the SNARE complex is initiated is unknown. Here we report that Sec3, a component of the exocyst complex that mediates vesicle tethering during exocytosis, directly interacts with the t-SNARE protein Sso2. This interaction promotes the formation of an Sso2-Sec9 ‘binary’ t-SNARE complex, the early rate-limiting step in SNARE complex assembly, and stimulates membrane fusion. The crystal structure of the Sec3-Sso2 complex suggests that Sec3 binding induces conformational changes of Sso2 that are crucial for the relief of its auto-inhibition. Interestingly, specific disruption of the Sec3–Sso2 interaction in cells blocks exocytosis without affecting the function of Sec3 in vesicle tethering. Our study reveals an activation mechanism for SNARE complex assembly, and uncovers a role of the exocyst in promoting membrane fusion in addition to vesicle tethering.

Suggested Citation

  • Peng Yue & Yubo Zhang & Kunrong Mei & Shaoxiao Wang & Johannes Lesigang & Yueyao Zhu & Gang Dong & Wei Guo, 2017. "Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion," Nature Communications, Nature, vol. 8(1), pages 1-12, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14236
    DOI: 10.1038/ncomms14236
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    Cited by:

    1. Di-Ao Liu & Kai Tao & Bin Wu & Ziyan Yu & Malwina Szczepaniak & Matthew Rames & Changsong Yang & Tatyana Svitkina & Yueyao Zhu & Fengyuan Xu & Xiaolin Nan & Wei Guo, 2023. "A phosphoinositide switch mediates exocyst recruitment to multivesicular endosomes for exosome secretion," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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