@article{86976,
  keywords = {Crystallography, X-Ray, Membrane Proteins, Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae, Transport Vesicles, SNARE Proteins, Endoplasmic Reticulum},
  author = {Yi Ren and Calvin Yip and Arati Tripathi and David Huie and Philip Jeffrey and Thomas Walz and Frederick Hughson},
  title = {A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1.},
  abstract = {<p>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.</p>
},
  year = {2009},
  journal = {Cell},
  volume = {139},
  pages = {1119-29},
  month = {12/2009},
  issn = {1097-4172},
  doi = {10.1016/j.cell.2009.11.002},
  language = {eng},
}