BAIT

BET3

TRAPP complex core subunit BET3, L000004057, YKR068C
Core component of transport protein particle (TRAPP) complexes I-III; TRAPP complexes are related multimeric guanine nucleotide-exchange factors for the GTPase Ypt1, regulating ER-Golgi traffic (TRAPPI), intra-Golgi traffic (TRAPPII), endosome-Golgi traffic (TRAPPII and III) and autophagy (TRAPPIII); hydrophilic homodimeric protein that acts in conjunction with SNARE proteins in targeting and fusion of ER to Golgi transport vesicles
GO Process (2)
GO Function (1)
GO Component (4)
Saccharomyces cerevisiae (S288c)
PREY

BET3

TRAPP complex core subunit BET3, L000004057, YKR068C
Core component of transport protein particle (TRAPP) complexes I-III; TRAPP complexes are related multimeric guanine nucleotide-exchange factors for the GTPase Ypt1, regulating ER-Golgi traffic (TRAPPI), intra-Golgi traffic (TRAPPII), endosome-Golgi traffic (TRAPPII and III) and autophagy (TRAPPIII); hydrophilic homodimeric protein that acts in conjunction with SNARE proteins in targeting and fusion of ER to Golgi transport vesicles
GO Process (2)
GO Function (1)
GO Component (4)
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

Organization and Assembly of the TRAPPII Complex.

Choi C, Davey M, Schluter C, Pandher P, Fang Y, Foster LJ, Conibear E

Current models suggest that TRAPP tethering complexes exist in two forms. Whereas the seven-subunit TRAPPI complex mediates ER-to-Golgi transport, TRAPPII contains three additional subunits (Trs65, Trs120 and Trs130) and is required for distinct tethering events at Golgi membranes. It is not clear how TRAPPII assembly is regulated. Here, we show that Tca17 is a fourth TRAPPII-specific component, and that Trs65 ... [more]

Unknown Feb. 24, 2011; 0(0); [Pubmed: 21453443]

Throughput

  • Low Throughput

Curated By

  • BioGRID