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Dev Cell. 2009 Sep;17(3):403-16. doi: 10.1016/j.devcel.2009.07.012.

A link between ER tethering and COP-I vesicle uncoating.

Author information

1
Department Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, D37077, Germany.

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.

PMID:
19758564
DOI:
10.1016/j.devcel.2009.07.012
[Indexed for MEDLINE]
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