BAIT

COP1

RET1, SEC33, SOO1, L000002603, YDL145C
Alpha subunit of COPI vesicle coatomer complex; complex surrounds transport vesicles in the early secretory pathway
GO Process (2)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

RER1

L000001613, YCL001W
Protein involved in retention of membrane proteins; including Sec12p, in the ER; localized to Golgi; functions as a retrieval receptor in returning membrane proteins to the ER
Saccharomyces cerevisiae (S288c)

Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

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

Zink S, Wenzel D, Wurm CA, Schmitt HD

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 ... [more]

Dev. Cell Sep. 01, 2009; 17(3);403-16 [Pubmed: 19758564]

Throughput

  • Low Throughput

Curated By

  • BioGRID