The majority of yki protein is cytoplasmic. To avoid isolating these cytoplasmic factors and instead identify proteins involved in yki transcriptional functions, yki was immunoprecipitated from nuclear extracts.

Source was nuclear extract of S2 cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Mutation of yki wts-phosphorylation sites or the yki WW domain does not disrupt this interaction.

Source was nuclear extract of S2 cell line; bait produced from transfected construct; prey produced from transfected construct.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

Mutation of yki wts-phosphorylation sites or the yki WW domain does not disrupt this interaction.

No difference in yki-Trl interaction with different yki isoforms including or excluding exon 3.

Source was cell extract of S2R+ cell line; bait produced from transfected construct; prey produced from transfected construct.