BAIT

MEG-3

gei-12, CELE_F52D2.4, F52D2.4
gei-12 encodes a novel protein that affects embryonic viability and development of the hypodermis; interacts with GEX-3 in yeast two-hybrid assays, and is expressed in all somatic cells.
GO Process (1)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Caenorhabditis elegans
PREY

GSK-3

CELE_Y18D10A.5, sgg-1, Y18D10A.5
gsk-3 encodes the C. elegans glycogen synthase kinase ortholog; during embryonic development, GSK-3 functions in the Wnt signaling pathway that restricts specification of mesendodermal tissue to the appropriate blastomere; GSK-3 also functions in a Wnt pathway that regulates anteroposterior axon guidance; GSK-3 plays a role in regulating the oocyte-to-embryo transition, by phosphorylating and negatively regulating the OMA-1 zinc finger protein, and in regulation of the oxidative stress response pathway by phosphorylating SKN-1, thereby excluding it from intestinal nuclei; GSK-3, along with MOM-5/Frizzled and APR-1/APC is also required for distal tip cell migration in the gonad and for the engulfment of apoptotic cells, indicating that the Wnt pathway signals to CED-10/Rac to regulate cytoskeletal rearrangement during different cellular processes; GSK-3 can be phosphorylated by murine ERK2 in vitro, suggesting that it is a substrate for the RTK-RAS-ERK pathway in vivo; consistent with this, GSK-3 phosphorylation is absent in mpk-1 mutant animals.
Caenorhabditis elegans

Affinity Capture-MS

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 is identified by mass spectrometric methods.

Publication

Novel LOTUS-domain proteins are organizational hubs that recruit C. elegans Vasa to germ granules.

Cipriani PG, Bay O, Zinno J, Gutwein M, Gan HH, Mayya VK, Chung G, Chen JX, Fahs H, Guan Y, Duchaine TF, Selbach M, Piano F, Gunsalus KC

We describe MIP-1 and MIP-2, novel paralogous C. elegans germ granule components that interact with the intrinsically disordered MEG-3 protein. These proteins promote P granule condensation, form granules independently of MEG-3 in the postembryonic germ line, and balance each other in regulating P granule growth and localization. MIP-1 and MIP-2 each contain two LOTUS domains and intrinsically disordered regions and ... [more]

Elife Dec. 05, 2020; 10(); [Pubmed: 34223818]

Quantitative Score

  • 0.738792473 [t_sam]

Throughput

  • High Throughput

Additional Notes

  • High confidence interactions were identified using a measure that combined fold-change of prey abundance as well as the p-value of a Student's t-test for experimental versus control purifications. Hit proteins were identified according to their p-value from the t SAM statistic as previously described (Chen et al., 2016). The t SAM statistic of the enrichment is provided in the score column.

Curated By

  • BioGRID