Analysis of mutants in chaoptin, a photoreceptor cell-specific glycoprotein in Drosophila, reveals its role in cellular morphogenesis.

Monoclonal antibody 24B10 (MAb24B10) specifically stains photoreceptor neurons in D. melanogaster. It recognizes a 160 kd glycoprotein localized to the extracellular face of the plasma membrane. Using an immunoscreen, we identified two mutations in the encoding gene that cause microvillar disorganization in developing rhabdomeres and disruption of the closely apposed membranes of adjacent cells. In accordance with the mutant phenotype, we have renamed this genetic locus chaoptic and the encoded glycoprotein, chaoptin. Immunoelectron microscopy indicates that chaoptin is distributed along the length of the microvillus. This localization and the morphological abnormalities in mutants support the hypothesis that chaoptin may mediate adhesion between closely apposed membranes. In principle, the immunoscreen utilized here can be used to identify mutations in any gene in Drosophila for which antibodies to the gene product are available.