SNAREs pp 175-189 | Cite as

Analysis of the Role of Sec3 in SNARE Assembly and Membrane Fusion

  • Kunrong Mei
  • Peng Yue
  • Wei GuoEmail author
Part of the Methods in Molecular Biology book series (MIMB, volume 1860)


Intracellular membrane fusion is mediated by the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins that are highly conserved and tightly regulated by a variety of factors. The exocyst complex is one of the multi-subunit tethering complexes and functions in the tethering of the secretory vesicles to the plasma membrane. We have found that the yeast Sec3, a subunit of the exocyst, binds to the t-SNARE protein Sso2 and promotes its interaction with another t-SNARE protein, Sec9. Here, we describe the structural analysis and in vitro membrane fusion assays, by which we found that Sec3 binding leads to a conformational change within Sso2, and facilitates SNARE assembly and the membrane fusion.

Key words

Sec3 Soluble N-ethylmaleimide-sensitive factor attachment protein receptor Sso2 Sec9 Structure analysis Liposome Membrane fusion 



We thank Shelby Wilkinson for helpful suggestions. We also thank the Gang Dong lab for solving the structure of the Sec3N-Sso2 complex. The work in W. G. lab is supported by National Institutes of Health R01 grant GM111128.


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© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Department of BiologyUniversity of PennsylvaniaPhiladelphiaUSA

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