baz phosphorylation site bind pdz of sdt to recruit sdt to pm. Phosphorylation of baz causes it to dissociate from sdt. Non-phosphorylatable baz blocks dissociation causing mutation similar to crb and sdt. crb cytoplasmic domain binds pdz domain of sdt and sdt recruit patj and lin-7 to apical complex. dlg/lgl/scrib localize to lateral pm and antagonize crb-sdt complex, restricting apical expansion. wt baz-gfp and bazs980e-gfp shows the same localization basal to crb-sdt. Phosphorylated bazs980-p was concentrated in most apical part, sometimes with/without crb-sdt. wt baz-gfp and bazs980e-gfp but not bazs980a-gfp rescued maternal and zygotic baz lethality. Overexpression of bazs980a-gfp is similar to crb and sdt. overexpression of bazs980a-gfp caused formation of aggregate containing de-cad, arm, -cat, bazs980a-gfp overexpression caused cells to round up and die of apoptosis. However, those lacking pm targeting signal was not dominant, showing bazs980a-gfp must be at pm to be dominant.