Abstract
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.
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Acknowledgments
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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Mei, K., Yue, P., Guo, W. (2019). Analysis of the Role of Sec3 in SNARE Assembly and Membrane Fusion. In: Fratti, R. (eds) SNAREs. Methods in Molecular Biology, vol 1860. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8760-3_10
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DOI: https://doi.org/10.1007/978-1-4939-8760-3_10
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