Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey from embryo cDNA expression library).

Mutation of phosphorylated Tyr residue in InR disrupts the interaction with dock.

None of the individual SH3 domains of dock bind InR, but together the three SH3 domains of dock bind to InR as strongly as the C-terminal dock SH2 domain binds InR.

Two-hybrid system: yeast GAL4-BD/VP16-AD

The intracellular domain of InR autophosphorylated in yeast cells.

Source was adult heads of wild-type fly line; bait produced from endogenous gene; prey produced from endogenous gene.

Authors used an antibody to human NCK that recognized endogenous dock in flies.

Source was larval brain and eye-antennal discs of wild-type fly line; bait produced from endogenous gene; prey produced from endogenous gene.

Authors used an antibody to human NCK that recognized endogenous dock in flies.

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

Phosphorylated InR was detected in anti-Myc immunoprecipitates from cells transfected with dock-Myc alone or with dock-Myc and a substrate trap version of Ptp61F with a C237S mutation.

Source was yeast cell line; bait produced as transgenic fusion protein; prey produced as transgenic fusion protein (prey was previously cloned reagent).

Two-hybrid system: yeast GAL4-BD/VP16-AD