Interaction inferred from the ability of excited CFP to induce YFP fluorescence.

fu dimerization is activated by treatment with hh-containing conditioned medium or expression of activated smo.

Bait expressed in transfected cells.

Prey expressed in transfected cells.

Interaction inferred from the ability of excited CFP to induce YFP fluorescence.

fu dimerization in the wing disc is strongest near the anterior-posterior compartment boundary.

Bait derived from a transgenic line carrying a CFP-tagged UAS-cos construct, P{UAS-fu.CFP}.

Bait derived from a transgenic line carrying a YFP-tagged UAS-cos construct, P{UAS-fu.YFP}.

Source was S2 cell line transfected with tagged fu constructs.

Separate molecules tagged with CFP and YFP; assaying homodimerization. FRET signal low in absence of hh protein, but high in presence of hh protein (in cell culture medium). Similar results with C-terminal fluorescent tags.

Source was wing discs from transgenic line carrying tagged fu constructs.

Separate molecules tagged with CFP and YFP; assaying homodimerization.

The regulatory domain of fu binds its catalytic domain.

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

Interaction in vitro; bait and prey produced as recombinant fusion proteins in baculovirus system.

co-IPs carried out with either antibody specific to fu kinase domain or fu C-terminal domain demonstrating that the two domains interact with each other.