Reference: Mei K, et al. (2019) Analysis of the Role of Sec3 in SNARE Assembly and Membrane Fusion. Methods Mol Biol 1860:175-189

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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.

Reference Type
Journal Article | Research Support, N.I.H., Extramural
Authors
Mei K, Yue P, Guo W
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