BAIT

RRT2

DPH7, ERE1, diphthamide synthase, YBR246W
Methylesterase performing penultimate step of diphthamide biosynthesis; hydrolyzes methylated diphthine to produce diphthine and allows Dph6-catalyzed amidation reaction to occur; deletion leads to resistance to sordarin and accumulation of methylatediphthine; WD40 domain-containing protein; involved in endosomal recycling; forms complex with Rtt10p that functions in retromer-mediated pathway for recycling internalized cell-surface proteins
GO Process (2)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

RTT10

ERE2, TRM734, YPL183C
WD40 domain-containing protein involved in endosomal recycling; forms a complex with Rrt2p that functions in the retromer-mediated pathway for recycling internalized cell-surface proteins; interacts with Trm7p for 2'-O-methylation of N34 of substrate tRNAs; has a role in regulation of Ty1 transposition; human ortholog is WDR6
GO Process (1)
GO Function (0)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Cellular Component

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

Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the retromer-mediated endosomal recycling pathway.

Shi Y, Stefan CJ, Rue SM, Teis D, Emr SD

Regulated secretion, nutrient uptake, and responses to extracellular signals depend on cell-surface proteins that are internalized and recycled back to the plasma membrane. However, the underlying mechanisms that govern membrane protein recycling to the cell surface are not fully known. Using a chemical-genetic screen in yeast, we show that the arginine transporter Can1 is recycled back to the cell surface ... [more]

Unknown Aug. 31, 2011; 0(0); [Pubmed: 21880895]

Throughput

  • Low Throughput

Curated By

  • BioGRID