Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system (prey from embryo cDNA expression library).

One of 28 positive clones (from 500,000 plaques screened) corresponded to Dab. Mutation of the drk SH2 domain (R85K) did not affect binding to Dab.

Bait GST-drk protein was [32]P labeled in vitro at an engineered PKA site in the linker, and used to probe a λgt11 cDNA expression library.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey derived from transfected S2 cell extract.

Expression of constitutively active sev kinase in S2 cells bypasses the requirement for the drk SH3 domain in Dab binding. Given that sev leads to tyrosine phosphorylation of Drk, the authors suggest that SH3-independent binding of drk-Dab is mediated by the drk SH2 domain.

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

Mutation of the drk SH2 domain (R85K) did not affect binding to Dab.

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

Overall SAINT probability of interaction = 1.