Bait expressed in transfected cells.

Prey expressed in transfected cells.

Dimerization of N-terminally tagged smo proteins is hh-independent, while dimerization of C-terminally tagged smo is hh-dependent.

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

Bait derived from transgenic line carrying CFP-tagged UAS-smo construct, P{UAS-smo.CFP.N}.

Prey derived from transgenic line carrying YFP-tagged UAS-smo construct, P{UAS-smo.YFP.N}.

Dimerization of N-terminally tagged smo proteins is hh-independent, while dimerization of C-terminally tagged smo is strongest near sources of endogenous hh.

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

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

Dimerization of N-terminally tagged smo proteins is hh-independent, while dimerization of C-terminally tagged smo is hh-dependent.

Phosphomimetic mutations of Serine residues to Aspartate in all three phosphorylation clusters of the smo C-terminal tail confer hh-independent smo dimerization.

Bait expressed in transfected cells.

Prey expressed in transfected cells.

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

Dimerization of N-terminally tagged smo proteins is hh-independent, while dimerization of C-terminally tagged smo is strongest near sources of endogenous hh.

Bait derived from transgenic line carrying CFP-tagged UAS-smo construct, P{UAS-smo.CFP.N}.

Prey derived from transgenic line carrying YFP-tagged UAS-smo construct, P{UAS-smo.YFP.N}.

Interaction of smo C-terminus with smo third intracellular loop inferred from the ability of excited CFP to induce YFP fluorescence.

Interaction of smo C-terminus with third intracellular loop of smo is inhibited by addition of hh-containing conditioned medium or smo mutations that activate the hh pathway.

Protein expressed in transfected cells.

Interaction of smo C-terminus with smo third intracellular loop inferred from the ability of excited CFP to induce YFP fluorescence.

Interaction of smo C-terminus with third intracellular loop of smo is reduced near sources of endogenous hh.

Protein derived from transgenic line carrying a CFP- and YFP-tagged UAS-smo construct, P{UAS-smo.CFP.L3.YFP.C}.

Pull down of GST-smo-SAID region.

Bait expressed and purified from bacteria.

Prey expressed in transfected cells.

Phosphorylation of smo C-terminal by PKA and CKI inhibits interaction with smo autoinhibitory domain (SAID).

Mutations that activate smo activity abolish the interaction of the smo C-terminal tail with the smo SAID region.

Pull down of GST-smo-SAID region.

Bait expressed and purified from bacteria.

Prey derived from in vitro translation.

Phosphorylation of smo C-terminal by PKA and CKI inhibits interaction with smo autoinhibitory domain (SAID).

Mutations that activate smo activity abolish the interaction of the smo C-terminal tail with the smo SAID region.

Source was live S2 cells; proteins produced from transfected constructs.

Knock-down of Gprk2 activity decreases FRET signal; Treating cells with hh increases signal.

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

Over expression of Gprk2 in absence of phosphorylation allows interaction; Knock-down of Gprk2 activity abolishes interaction of phosphomimetic smo SD mutant.

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

Over expression of Gprk2 in absence of phosphorylation allows interaction; Knock-down of Gprk2 activity abolishes interaction of phosphomimetic smo SD mutant.

smo molecules in the same cell are tagged with CFP or YFP, and the interaction of smo molecules is inferred from the ability of excited CFP to induce YFP fluorescence.

Treatment of cells with conditioned medium containing hh protein induces smo dimerization.

Phosphomimetic mutations of Serine residues to Aspartate in all three phosphorylation clusters of the smo C-terminal tail confer hh-independent smo dimerization.

Protein expressed in transfected cells.

Source was live S2R+ cells; proteins produced from transfected constructs.

smo phosphomimetic mutant S667D,S670D,S673D,S687D,S690D,S693D,S740D,S743D,S746D used. Co-expression of Gprk2 increases smo dimerization.

Source was live S2 cells; fluorescence donor produced from transfected construct; fluorescence acceptor produced from transfected construct.

Dimerization of mutant smo is much less resposive to treatment with hh and PI(4)P.