Zink S, et al. (2009) A link between ER tethering and COP-I vesicle uncoating. Dev Cell 17(3):403-16
Abstract: The yeast Dsl1p vesicle tethering complex, comprising the three subunits Dsl1p, Dsl3p, and Tip20p, is stably associated with three endoplasmic reticulum-localized Q-SNAREs and is believed to play a central role in the tethering and fusion of Golgi-derived COP-I transport vesicles. Dsl1p also interacts directly with COP-I subunits. We now show that binding of Dsl1p to COP-I subunits involves binding sites identical to those involved in interactions between COP-I subunits that stabilize the COP-I coat. Cells with defects in Dsl/SNARE complex function show massive accumulation of COP-I-coated vesicles in a cluster to which COP-II coat proteins are also recruited. Our results suggest that binding of Dsl/SNARE complex to the COP-I coat complex serves two functions: to mediate vesicle tethering and to assist the uncoating process by blocking domains in COP-I that drive repolymerization and the formation of large COP-I aggregates.
|Status: Published||Type: Journal Article | Research Support, Non-U.S. Gov't||PubMed ID: 19758564|
Topics addressed in this paper
Number of different genes curated to this paper: 17
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|Topics||Genes (#1 - 10 )|
|Protein Sequence Features|
|Topics||Genes (#11 - 17 )|