Source was intact S2 cells; bait produced from transfected construct; prey produced from transfected construct.

The N-Ser interaction requires Ca[2+].

S2 cells expressing N were mixed with S2 cells expressing Ser, and the formation of cell clusters containing both N and Ser expressing cells was assayed by immunofluorescence.

Binding of N to Ser is decreased in the presence of expressed fng.

Interaction in vitro; bait and prey produced as a recombinant fusion proteins in S2 cells

Binding of N to Ser is decreased in the presence of expressed fng.

ligand expressed on the surface of S2 cells (bait), AP tagged N purified from transfected S2 cells (prey).

Interaction in vitro; proteins produced from transfected constructs.

Coexpression of fng with N disrupts the N-Ser interaction.

Source was two separate S2 cell lines, one transfected with a tagged N construct and the other with a tagged Ser construct.

Cell-aggregation assay.

Alkaline-phosphatase-tagged Ser was collected from conditioned media and mixed with S2 cells expressing N. After extensive washing of cells, the amount of alkaline phosphatase bound to cells was measured.

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

The interaction of N with Ser is disrupted by the V361M mutation. However, this same mutation slightly increases binding of N to Dl.

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

Physical interaction of proteins expressed on the surface of cells is inferred from the aggregation of live cells.

Assay: cell aggregation. Expression of cis-Ser in the N cells competes with N interaction with trans-expressing Ser cells.

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

N, cno and Ser colocalize at the apical side of neuroepithelial cells, at the interface with surrounding glia.

Co-expression of fng with N decreased Ser binding; fng glycosyltransferase activity was required for decrease; mutation of N O-fucosylation site, T348V, abolishes fng mediated reduction of N-Ser binding.

Source was live S2 cells; bait produced from transfected construct; prey purified from medium of transfected cells.

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

Physical interaction of proteins expressed on the surface of cells is inferred from the aggregation of live cells. Co-expression of N in the same cells as Ser interferes with aggregation with N expressing cells. This interference is overcome by coexpressing fng with N and Ser.