Cell
Volume 139, Issue 6, 11 December 2009, Pages 1119-1129
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Article
A Structure-Based Mechanism for Vesicle Capture by the Multisubunit Tethering Complex Dsl1

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Summary

Vesicle trafficking requires membrane fusion, mediated by SNARE proteins, and upstream events that probably include “tethering,” an initial long-range attachment between a vesicle and its target organelle. Among the factors proposed to mediate tethering are a set of multisubunit tethering complexes (MTCs). The Dsl1 complex, with only three subunits, is the simplest known MTC and is essential for the retrograde traffic of COPI-coated vesicles from the Golgi to the ER. To elucidate structural principles underlying MTC function, we have determined the structure of the Dsl1 complex, revealing a tower containing at its base the binding sites for two ER SNAREs and at its tip a flexible lasso for capturing vesicles. The Dsl1 complex binds to individual SNAREs via their N-terminal regulatory domains and also to assembled SNARE complexes; moreover, it is capable of accelerating SNARE complex assembly. Our results suggest that even the simplest MTC may be capable of orchestrating vesicle capture, uncoating, and fusion.

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4

Present address: Laboratory of Cell Biology, The Rockefeller University, New York, NY 10065, USA

5

Present address: Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA