Characterization and mutant analysis of the Drosophila sema 5c gene.

Class V semaphorins are transmembrane glycoproteins characterised by the presence of thrombospondin type I (Tsp) repeats linked to their extracellular semaphorin domain. Sema 5C is the only class V semaphorin found in Drosophila. Dsema 5C RNA is maternally provided and its embryonic expression is prominent in the mesoderm and muscle attachment sites. Here, we show that DSema 5C exists in two protein isoforms as a result of alternative splicing and that both protein and RNA have similar expression patterns. Using a combination of various molecular markers, we show that the DSema 5C protein becomes enriched in mesodermal cells that would normally give rise to fat body and visceral structures. In late embryos, DSema 5C is expressed in segment boundary cells that would constitute subsets of muscle attachment sites. Both RNA and protein are excluded from the somatic precursors and the mature muscles. The expression data suggest DSema 5C localised to the epidermal component of muscle attachment sites. Mutations in Dsema 5C were isolated from a P-element excision screen and by blotting analysis. The Dsema 5C mutants are homozygous viable and show no obvious embryonic phenotypes, suggesting that the maternal and zygotic components of Dsema 5C are not essential for fly development.