3k8p
Structural basis for vesicle tethering by the Dsl1 complexStructural basis for vesicle tethering by the Dsl1 complex
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedVesicle 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. A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1.,Ren Y, Yip CK, Tripathi A, Huie D, Jeffrey PD, Walz T, Hughson FM Cell. 2009 Dec 11;139(6):1119-29. PMID:20005805[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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