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

The extracellular domain of Dscam1 was used for the interaction.

Source was cell extract of 293 cell line; bait produced from transfected construct; prey produced from transfected construct.

Dscam1 coimmunoprecipitates only the proteolytically processed sliN form, not the full length protein. This interaction was observed in 293 cells (which process sli) but not in COS cells (which do not process sli).

Deletion of the robo1 binding site in sli does not disrupt the sli-Dscam1 interaction.

COS cells expressing Dscam1 constructs (cytoplasmic domain replaced by His tag) were overlaid with conditioned media from 293 cells expressing sli. Cells were incubated for 1-2 hr, then fixed. Surface-bound ligand was assayed by immunofluorescence.

sli has at least two binding sites in the first five Ig domains of Dscam1 (not precisely identified in this study).

Deletion of the robo1 binding site in sli does not disrupt the sli-Dscam1 interaction.

Interaction in vitro; bait produced from transfected constructs in COS cells; prey derived from condition media of 293 cells.

Interaction in vitro; bait derived from conditioned media of stably transfected High Five cells; prey derived from conditioned media of baculovirus-infected High Five cells.

At least two sli binding sites in Dscam1 exist within Ig domains 1-4, but these were not precisely mapped.