BAIT

BAR-1

CELE_C54D1.6, pvl-1, spy-1, C54D1.6
bar-1 encodes a beta-catenin; during C. elegans development, BAR-1 likely functions as a transcriptional coactivator whose activity is required for Q neuroblast migration, P12 cell fate specification, and P3.p through P8.p vulval cell fate specification at two different stages of development; in specifying vulval cell fates, bar-1 interacts with Wnt and MAPK signaling pathways to regulate proper expression of the LIN-39 homeodomain transcription factor, overexpresion of which can partially rescue the bar-1 mutant phenotype; in yeast two-hybrid assays, BAR-1 interacts strongly with the POP-1/TCF transcription factor, and when fused to the Gal4 DNA binding domain, BAR-1 can function in yeast as a transcriptional coactivator; during larval development, BAR-1 expression begins in P3.p through P8.p at the late L1 stage and then disappears from these cells by the mid-L3 stage; BAR-1 is also expressed in P12, in the seam cells, and in cells of the somatic gonad; BAR-1 subcellular localization, assessed using an integrated transgene, reveals localization to the cytoplasm, nucleus, and cell junctions; genetic mosaic analyses indicate that, in P4.p and in P12, bar-1 acts cell autonomously to specify cell fates.
Caenorhabditis elegans
PREY

DPY-22

CELE_F47A4.2, mdt-12, psa-6, sop-1, F47A4.2
dpy-22 encodes a broadly expressed protein, homologous to the human transcriptional mediator protein TRAP230, which is involved in WNT and RAS signaling, as well as in dosage compensation; DPY-22 has a C-terminal glutamine-rich domain that is dispensable for inhibition of RAS-dependent cell differentiation, but is required for inhibition of BAR-1-dependent gene expression.
Caenorhabditis elegans

Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

Publication

EPIC: software toolkit for elution profile-based inference of protein complexes.

Hu LZ, Goebels F, Tan JH, Wolf E, Kuzmanov U, Wan C, Phanse S, Xu C, Schertzberg M, Fraser AG, Bader GD, Emili A

Protein complexes are key macromolecular machines of the cell, but their description remains incomplete. We and others previously reported an experimental strategy for global characterization of native protein assemblies based on chromatographic fractionation of biological extracts coupled to precision mass spectrometry analysis (chromatographic fractionation-mass spectrometry, CF-MS), but the resulting data are challenging to process and interpret. Here, we describe EPIC ... [more]

Nat. Methods Jul. 15, 2019; (); [Pubmed: 31308550]

Quantitative Score

  • 0.561 [Confidence Score]

Throughput

  • High Throughput

Additional Notes

  • High confidence protein interactions have an EPIC PPI score >= 0.5

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
BAR-1 DPY-22
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High4BioGRID
466545

Curated By

  • BioGRID