BAIT

SPA2

FUS6, PEA1, PPF1, L000001989, YLL021W
Component of the polarisome; functions in actin cytoskeletal organization during polarized growth; acts as a scaffold for Mkk1p and Mpk1p cell wall integrity signaling components; potential Cdc28p substrate; coding sequence contains length polymorphisms in different strains; SPA2 has a paralog, SPH1, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

PDR5

LEM1, STS1, YDR1, ATP-binding cassette multidrug transporter PDR5, L000001365, L000002136, L000002504, YOR153W
Plasma membrane ATP-binding cassette (ABC) transporter; multidrug transporter actively regulated by Pdr1p; also involved in steroid transport, cation resistance, and cellular detoxification during exponential growth; PDR5 has a paralog, PDR15, that arose from the whole genome duplication
GO Process (3)
GO Function (1)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

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

Quantitative proteomics reveals a Gα/MAPK signaling hub that controls pheromone-induced cellular polarization in yeast.

Waszczak N, DeFlorio R, Ismael A, Cheng N, Stone DE, Metodiev MV

The mating-specific yeast Gα controls pheromone signaling by sequestering Gβγ and by regulating the Fus3 MAP kinase. Disrupting Gα-Fus3 interaction leads to severe defects in chemotropism. Because Gα concentrates at the chemotropic growth site where Fus3 is required for the phosphorylation of two known targets, we screened for additional proteins whose phosphorylation depends on pheromone stimulation and Gα-Fus3 interaction. Using ... [more]

J Proteomics Jul. 24, 2019; 207();103467 [Pubmed: 31351147]

Throughput

  • Low Throughput

Curated By

  • BioGRID