SNARE proteins are essential for exocytosis, mediating the fusion of vesicles with their target membrane. Tethering factors play a key role in chaperoning SNARE assembly; however, the underlying molecular mechanisms are not well-understood. Here, Travis et al. report two crystal structures of a yeast tethering factor, the Dsl1 complex, bound with two SNARE proteins, revealing new insights into how tethering factors bridge vesicles to target membranes, recruit multiple SNARE proteins, trigger their conformational changes, and facilitate SNARE assembly. © 2020 Zhang and Yang.
Yongli Zhang, Jie Yang. Securing SNAREs for assembly. The Journal of biological chemistry. 2020 Jul 24;295(30):10136-10137
PMID: 32709759
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