Molecular characterization of Pegarn: a Drosophila homolog of UNC-51 kinase.

We have isolated and characterized the gene encoding a Drosophila melanogaster homolog of Caenorhabditis elegans UNC-51 (uncoordinated movement-51): Pegarn. Developmental Northern blot shows the Pegarn gene is expressed at all stages of development. The protein is detected throughout the Drosophila third instar larval central nervous system (CNS) in axons projecting out from the ventral ganglion and in the optic anlagen of the optic lobe.

Apolipophorin-III-like protein expressed in the antenna of the red imported fire ant, Solenopsis invicta Buren (Hymenoptera: Formicidae).

Antennal proteins of the male fire ant (Solenopsis invicta) were analyzed by two-dimensional gel electrophoresis, with the objective of identifying pheromone-binding proteins, which have not previously been found in ant antennae. The major low-molecular weight protein found in the male fire ant antenna was subjected to Edman degradation to determine the N-terminal amino acid sequence. Degenerate PCR primers based on this sequence were used to obtain a cDNA sequence corresponding to the full-length protein sequence.

pcdr, a novel gene with sexually dimorphic expression in the pigment cells of the Drosophila eye.

We report the molecular cloning and characterization of pcdr (pigment cell dehydrogenase reductase), a Drosophila visual system-specific gene with novel properties of spatial, temporal and sexual regulation. Short chain dehydrogenase/reductases are a family of proteins that catalyze mechanistically conserved dehydrogenase/reductase reactions in a wide range of cells and tissues. These enzymes are required in a variety of reactions ranging from steroid metabolism and prostaglandin synthesis to alcohol detoxification.

Defective intracellular transport is the molecular basis of rhodopsin-dependent dominant retinal degeneration.

Retinitis pigmentosa (RP) is a group of hereditary human diseases that cause retinal degeneration and lead to eventual blindness. More than 25% of all RP cases in humans appear to be caused by dominant mutations in the gene encoding the visual pigment rhodopsin. The mechanism by which the mutant rhodopsin proteins cause dominant retinal degeneration is still unclear.

Identification of two bone morphogenetic protein type I receptors in Drosophila and evidence that Brk25D is a decapentaplegic receptor.

Drosophila sequences at chromosomal positions 25D (Brk25D) and 43E (Brk43E) are similar to the TGF beta type I receptor serine/threonine kinases and are expressed broadly during embryogenesis. Brk25D binds dpp protein and bone morphogenetic protein 2 with high affinity. Mutations affecting Brk25D map to the gene thick veins and block the expression of two decapentaplegic-responsive (dpp-responsive) genes, dpp and labial, in the embryonic midgut.