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

Interaction of smo and cos increased upon treatment of cells with hh.

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

Interaction of smo and cos increased upon treatment of cells with hh.

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

Interaction of smo and cos increased upon treatment of cells with hh.

Source was cell extract of clone8 cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Interaction of smo and cos increased upon treatment of cells with hh.

Source was cell extract of clone8 cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Interaction of smo and cos increased upon treatment of cells with hh.

Source was cell extract of clone8 cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Interaction of smo and cos increased upon treatment of cells with hh.

Source was cell extract of clone8 cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Interaction of smo and cos increased upon treatment of cells with hh.

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/GAL4-AD

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

The interaction of smo and cos is not affected by the expression of hh in S2 cells.

Source was larval wing discs of transgenic fly line; bait produced from tagged transgenic construct; prey produced from endogenous gene.

Bait protein was fused to the motor domain of kinesin heavy chain (Khc), which targets the chimera to the plus end of microtubules. The ability of this chimera to recruit prey protein to the plus end of microtubules was taken as evidence of direct physical interaction.

Bait protein was fused to the motor domain of kinesin heavy chain (Khc), which targets the chimera to the plus end of microtubules. The ability of this chimera to recruit prey protein to the plus end of microtubules was taken as evidence of direct physical interaction.

Source was larval wing discs of transgenic fly line; bait produced from tagged transgenic construct; prey produced from transgenic construct.

Bait protein was fused to the motor domain of kinesin heavy chain (Khc), which targets the chimera to the plus end of microtubules. The ability of this chimera to recruit prey protein to the plus end of microtubules was taken as evidence of direct physical interaction.

Source was larval wing discs of transgenic fly line; bait produced from tagged transgenic construct; prey produced from transgenic construct.

Source was cell extract of CME-W1-Cl.8+ cell line; bait produced from transfected construct; prey produced from endogenous gene.

The cos S572 residue is phosphorylated upon hh treatment.

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

Phosphorylation of cos at residue S572 disrupts its interaction with smo in vitro, and destabilizes the protein in cells.

Interaction 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 interaction with cos.

Bait expressed in transiently transfected cells.

Prey expressed in transiently transfected cells.

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

Interaction of smo and cos in the wing disc is strongest near the anterior-posterior compartment boundary.

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

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

Source was S2 cell line transfected with tagged smo and cos constructs.

FRET signal increased with increasing levels of hh protein (in cell culture medium).

Source was cell extract of CME-W1-Cl.8+ cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Cells treated with hh.

Source was cell extract of CME-W1-Cl.8+ cell line; bait produced from endogenous gene; prey produced from endogenous gene.

Cells treated with hh. smo also found in immunoprecipitates with antibodies specific to cos phosphorylated at Ser572 or at Ser931, with greatest level of smo precipitating with cos phosphorylated at Ser931.

Bait expressed in transiently transfected cells.

Prey expressed in transiently transfected cells.

Treatment of cells with conditioned medium containing hh protein induces the smo-cos interaction.

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

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

smo mutant S667D,S670D,S673D,S687D,S690D,S693D,S740D,S743D,S746D allows interaction in the absence of hh treatment.

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

Co-expression of Gprk2 increases interaction.