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PubMed1987

Characterization of a Drosophila cDNA clone that encodes a 252-amino acid non-muscle tropomyosin isoform.

We report here the isolation and DNA sequence of a cDNA clone encoding a 252-amino acid non-muscle or cytoskeletal tropomyosin (cTm) isoform from Drosophila. The Drosophila cTm shows considerable homology with vertebrate cTm throughout the middle portion of the molecule. The amino-terminal end of the molecule, however, shows less homology and contains five more amino acids than the equine platelet and human tropomyosins. There is also a proline at position 6 in the Drosophila protein. The carboxyl-terminal 27 amino acids also show little homology with vertebrate non-muscle tropomyosins. This is a region of the molecule that shows considerably diversity among other Drosophila tropomyosins and vertebrate tropomyosins. A comparison of the DNA sequence of the cTm cDNA and a previously reported muscle tropomyosin II cDNA sequence shows regions of identical DNA sequence alternating with regions of nonidentical sequence, suggesting that both mRNAs are produced by alternate splicing of the same gene.

Amino Acid Sequence↗
PubMed1995

Drosophila gp210, an invertebrate nuclear pore complex glycoprotein.

Monoclonal antibodies were used to localize the putative Drosophila homolog of mammalian nuclear pore complex glycoprotein, gp210, to Drosophila nuclear pore complexes. Both immunofluorescence and immunoelectron microscopy were performed. To the best of our knowledge, this establishes Drosophila gp210 as the first invertebrate gp210 homolog. Results of developmental studies demonstrated that like nuclear lamin and DNA topoisomerase II, gp210 is found abundantly in nonnuclear form early in embryogenesis where it presumably fuels the rapid assembly of new nuclei. Unlike thse other two proteins, gp210 levels are maximal early after wich they decrease significantly; in addition, nonnuclear gp210 found in early Drosophila embryos is apparently associated with membrane vesicles. These results have implications for understanding the regulation of higher eukaryotic nuclear pore complex behavior through development as well as for determining gp210 function genetically.

Animals↗
PubMed1995

Genetic analysis of Drosophila neurons: Shal, Shaw, and Shab encode most embryonic potassium currents.

In this study, we perform the first genetic analysis of K+ currents in Drosophila embryonic neurons revealing the identity of the currents present. Unlike muscles, where the presence of Shaker is obvious, Shaker currents are not detectable in these neurons. In contrast, we show that Shal is as important in these neuronal cell bodies as Shaker is in muscles. Only three single-channel currents were found, all of which are genetically separable. Shal encodes a 4 pS transient channel. Whole-cell Shal currents have a wide variety of inactivation rates which, in contrast to a mechanism such as heteromultimer formation, is due to single Shal channels assuming different gating modes. Shaw encodes a 42 pS noninactivating channel distinctive for its extremely low voltage sensitivity; Shaw channels have a total equivalent gating charge of 0.90 e- charges, in sharp contrast to 7 e- reported for Shaker channels. An 11 pS slowly inactivating channel also present in these neurons may be encoded by the Shab gene. Thus, of four voltage-dependent K+ channel genes now cloned in Drosophila, all except Shaker appear to be expressed in the cell bodies of these neurons. It is only in Drosophila that a study such as this one can be done. Because Drosophila contains only a single member of each of the four subfamilies of K+ channel genes (unlike mammals), we can eliminate an entire subfamily with a mutation to a single gene. Here, we have examined the effect of eliminating each of three subfamilies. Such a task is presently impossible to accomplish in any mammalian system.

Animals↗
PubMed1993

Wingless, the Drosophila homolog of the proto-oncogene Wnt-1, can transform mouse mammary epithelial cells.

The segment polarity gene wingless is the Drosophila ortholog of mouse Wnt-1, a proto-oncogene capable of causing transformation of mammary epithelial cells. These two genes presently represent the best studied members of the Wnt gene family. To evaluate the functional significance of the sequence conservation between wingless and Wnt-1, we have examined the effects of expressing the Drosophila gene in mouse mammary epithelial cell lines. wingless induced morphological transformation, focus formation, and mitogenesis in confluent cultures of these cells, with resulting phenotypes comparable to those obtained with mouse Wnt-1. In addition, RAC311c mammary cells expressing wingless were tumorigenic, indicating that the Drosophila gene is capable of inducing full neoplastic transformation. In cell co-culture experiments, wingless caused transformation via a paracrine mechanism, consistent with the extracellular location of its product and its proposed mechanism of action in Drosophila embryos. Our results indicate that wingless is functionally analogous to Wnt-1 in these mammary cell transformation assays and imply a striking conservation in the properties of the two gene products and their mechanisms of action.

Animals↗
PubMed1994

Specificity of bone morphogenetic protein-related factors: cell fate and gene expression changes in Drosophila embryos induced by decapentaplegic but not 60A.

Reported assays of the bone morphogenetic proteins (BMPs) have not in general revealed specific functions for the different proteins, belying the specificity implied by the evolutionary conservation and distinct expression patterns of the genes encoding BMPs. We have used assays of developmental function to show that the two Drosophila homologues of the BMPs, decapentaplegic (dpp) and 60A, that both induce ectopic bone formation in mammalian assay systems, have distinct effects in Drosophila development. A binary expression system using the yeast transcriptional activator GAL4 directed identical patterns of tissue and temporally specific dpp and 60A expression. When dpp enhancer elements drove GAL4 expression, GAL4-responsive dpp transgenes rescued dpp mutant phenotypes, but GAL4-responsive 60A transgenes did not. Ectopic ectodermal expression of dpp during gastrulation respecified the dorsal/ventral pattern of the embryo. In contrast, ectopic 60A expression had no detectable effects on embryonic development but led to defects in adult structures or lethality during metamorphosis. Expression of 60A in cells expressing dpp did not interfere with dpp functions, indicating that dysfunctional heterodimers did not form at sufficient levels to inhibit dpp. These specific developmental responses in Drosophila indicate that in vivo functions of BMP-like factors can be more specific than indicated by the ectopic bone formation assays and that the Drosophila embryo provides an assay system sensitive to the structural differences that contribute to BMP specificity in vivo.

Amino Acid Sequence↗
PubMed1994

Conservation of regulated alternative splicing and identification of functional domains in vertebrate homologs to the Drosophila splicing regulator, suppressor-of-white-apricot.

Although several splicing regulatory proteins have been identified in Drosophila through characterization of various genetic mutations, including sex-lethal, transformer, transformer-2, suppressor-of-white-apricot (su(wa)), and possibly suppressor-of-sable, none of these have been identified in vertebrates. We describe the cloning and characterization of human (HsSWAP) and mouse (MmSWAP) homologs of the su(wa) gene. Comparison of the Drosophila and mammalian proteins reveals five highly homologous regions, including an arginine/serine-rich domain and two repeated modules that are homologous to regions in the constitutive splicing factor, SPP91/PRP21. These modules thus define a new motif likely important in the regulatory and constitutive splicing functions of these proteins. The Drosophila su(wa) gene autoregulates its expression by control of splicing of its first two introns. Comparison of mammalian and Drosophila SWAP mRNAs revealed that the splice junctions of these regulated introns are precisely conserved, showing definitively that these genes are ancestrally related. Moreover, mammalian SWAP mRNAs are also alternatively spliced at the same splice sites, showing that mammalian SWAP expression is regulated (presumably autogenously) by control of splicing of these two introns. These several structural features therefore strongly suggest that the mammalian SWAP gene functions as a vertebrate alternative splicing regulator.

Alternative Splicing↗
PubMed1993

An 18-bp element in the 5' untranslated region of the Drosophila beta 2 tubulin mRNA regulates the mRNA level during postmeiotic stages of spermatogenesis.

During Drosophila spermatogenesis transcriptional activity is mainly restricted to premeiotic stages. Translation during sperm morphogenesis, however, proceeds for several days, requiring a high stability for mRNAs translated postmeiotically. We studied expression of the Drosophila beta 2 tubulin gene, which is expressed solely in the male germ line from the primary spermatocyte stage onwards. Cis-acting elements involved in the regulation of mRNA levels were investigated in transgenic fly strains. In adult testes, mRNA amounts from beta 2-lacZ fusion genes in the presence of an 18-bp AT-rich element, termed beta 2DE1, are elevated about threefold. The element is present at about the same position in the 5' untranslated regions of the beta 2 tubulin genes of the distantly related species Drosophila melanogaster and Drosophila hydei. Changing the position of the element on the mRNA reduces the stabilizing effect, while inversion of the beta 2DE1 abolishes its function. The element also acts in a combination with the beta 1 tubulin transcription start site, and the beta 2UE1, which is required to achieve tissue-specific expression. In all experiments done, the comparison of premeiotic with postmeiotic stages strongly implies that this element is involved in regulating mRNA stability. This mRNA stabilizing element acts in a position-independent manner and also on a heterologous mRNA, showing its autonomous functional activity.

Animals↗
PubMed1994

The SH2-like Akt homology (AH) domain of c-akt is present in multiple copies in the genome of vertebrate and invertebrate eucaryotes. Cloning and characterization of the Drosophila melanogaster c-akt homolog Dakt1.

The Akt proto-oncogene encodes a serine-threonine protein kinase whose carboxyterminal catalytic domain is closely related to the catalytic domains of all the known members of the protein kinase C (PKC) family. Akt, however, differs from PKC in its N-terminal region which contains a domain related distantly to the SH2 domain of cytoplasmic tyrosine kinases and other signalling proteins, which we have named Akt homology (AH) domain. Low stringency hybridization of a c-akt AH probe to a panel of genomic DNAs from vertebrate and invertebrate eucaryotes detected multiple DNA bands (perhaps multiple genes) in all tested species. Drosophila DNA contains at least three hybridizing DNA bands. One of them was cloned, and found by sequence analysis, to define an Akt related gene (Dakt1). Comparison between the coding regions of c-akt and Dakt1 revealed 64.6% identity at the nucleotide level and 76.5% similarity at the amino acid level. The highest degree of homology was detected in the AH domain (68.3% similarity at the amino acid level) and the catalytic domain (83.3% similarity). Additional sequence comparisons revealed that the amino acid similarity between the catalytic domains of Dkt1 and the three known members of the Drosophila protein kinase C (PKC) family, Dpkc1, Dpkc2 and Dpkc3, is 68%, 63.6% and 67.1%, respectively. Dakt1 was mapped to Drosophila chromosome 3R 89BC. Its expression is subject to developmental regulation with the highest levels detected within the fourth hour of embryonic development. These results confirm that the AH domain of Akt defines new protein families in both vertebrate and invertebrate eucaryotes. The high degree of homology between the catalytic domains of Dkt1 and the three known members of the Drosophila PKC family suggests an evolutionarily conserved functional relationship between the members of the two families.

Amino Acid Sequence↗
PubMed1993

An invertebrate calcium-binding protein of the calbindin subfamily: protein structure, genomic organization, and expression pattern of the calbindin-32 gene of Drosophila.

Antisera against vertebrate calcium-binding proteins cross-react with Drosophila nervous and muscle tissue. We have used an antiserum against carp parvalbumin to isolate from a Drosophila head cDNA library immunopositive expression clones. Tissue in situ hybridization identified a clone that labeled specific neurons and muscles similar to the parvalbumin-like immunohistochemical staining pattern. Five independent cDNAs derive from an mRNA whose open reading frame codes for a 310 amino acid polypeptide. Sequence analysis identifies six EF-hand calcium-binding domains and reveals 42% and 37% homology to chicken calretinin and calbindin D-28k, respectively. Since the positions of 9 out of 10 introns within the ORF are conserved from the Drosophila gene to both vertebrate genes, we conclude that we have identified the first invertebrate member of the calbindin sub-family of calcium-binding protein genes of the EF-hand homolog family. The calbindin-32 gene (cbn) maps to 53E on the second chromosome. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. The cloning of a Drosophila homolog to vertebrate neuronal Ca(2+)-binding proteins opens new routes to study the so far largely elusive function of these brain molecules.

Amino Acid Sequence↗
PubMed1996

The structure-function relationships in Drosophila neurotactin show that cholinesterasic domains may have adhesive properties.

Neurotactin (Nrt), a Drosophila transmembrane glycoprotein which is expressed in neuronal and epithelial tissues during embryonic and larval stages, exhibits heterophilic adhesive properties. The extracellular domain is composed of a catalytically inactive cholinesterase-like domain. A three-dimensional model deduced from the crystal structure of Torpedo acetylcholinesterase (AChE) has been constructed for Nrt and suggests that its extracellular domain is composed of two sub-domains organized around a gorge: an N-terminal region, whose three-dimensional structure is almost identical to that of Torpedo AChE, and a less conserved C-terminal region. By using truncated Nrt molecules and a homotypic cell aggregation assay which involves a soluble ligand activity, it has been possible to show that the adhesive function is localized in the N-terminal region of the extracellular domain comprised between His347 and His482. The C-terminal region of the protein can be removed without impairing Nrt adhesive properties, suggesting that the two sub-domains are structurally independent. Chimeric molecules in which the Nrt cholinesterase-like domain has been replaced by homologous domains from Drosophila AChE, Torpedo AChE or Drosophila glutactin (Glt), share similar adhesive properties. These properties may require the presence of Nrt cytoplasmic and transmembrane domains since authentic Drosophila AChE does not behave as an adhesive molecule when transfected in S2 cells.

Acetylcholinesterase↗
PubMed1998

Regulated spacing of synapses and presynaptic active zones at larval neuromuscular junctions in different genotypes of the flies Drosophila and Sarcophaga.

Synapses at larval neuromuscular junctions of the flies Drosophila melanogaster and Sarcophaga bullata are not distributed randomly. They have been studied in serial electron micrographs of two identified axons (axons 1 and 2) that innervate ventral longitudinal muscles 6 and 7 of the larval body wall. The following fly larvae were examined: axon 1--wild-type Sarcophaga and Drosophila and Drosophila mutants dunce(m14) and fasII(e76), a hypomorphic allele of the fasciclin II gene; and axon 2--drosophila wild-type, dunce(m14), and fasII(e76). These lines were selected to provide a wide range of nerve terminal phenotypes in which to study the distribution and spacing of synapses. Each terminal varicosity is applied closely to the underlying subsynaptic reticulum of the muscle fiber and has 15-40 synapses. Each synapse usually bears one or more active zones, characterized by dense bodies that are T-shaped in cross section; they are located at the presumed sites of transmitter release. The distribution of synapses was characterized from the center-to-center distance of each synapse to its nearest neighbor. The mean spacing between nearest-neighbor pairs ranged from 0.84 microm to 1.05 microm for axon 1, showing no significant difference regardless of genotype. The corresponding values for axon 2, 0.58 microm to 0.75 microm, were also statistically indistinguishable from one another in terminals of different genotype but differed significantly from the values for axon 1. Thus, the functional class of the axon provides a clear prediction of the spacing of its synapses, suggesting that spacing may be determined by the functional properties of transmission at the two types of terminals. Individual dense bodies were situated mostly at least 0.4 microm away from one another, suggesting that an interaction between neighboring active zones could prevent their final positions from being located more closely.

Animals↗
PubMed1996

Chicken homeobox gene Prox 1 related to Drosophila prospero is expressed in the developing lens and retina.

Prox 1 is the vertebrate homolog of Drosophila prospero, a gene known to be expressed in the lens-secreting cone cells of fly ommatidia. Chicken Prox 1 cDNAs were isolated from 14 day embryonic chicken lenses, and a complete open reading frame encoding an 83 kDa protein was elucidated. The homeodomains of chicken and mouse Prox 1 are identical at the amino acid level and are 65-67% similar to the homeodomains of Drosophila and C. elegans prospero. The homology between these proteins extends beyond the homeodomain. There is 56% identity between chicken Prox 1 and Drosophila prospero in the C-terminal region downstream of the homeodomain, whereas there is little similarity upstream of the homeodomain. Prox 1 is expressed most actively in the developing lens and midgut and at lower levels in the developing brain, heart, muscle, and retina. cDNA sequencing has established that there are alternatively spliced forms of the single Prox 1 gene, which probably account for the two abundant RNAs of about 2 and 8 kb and two less abundant RNAs close to 3.5 kb in length in the lens. In the lens fibers, only the shortest mRNA was present, whereas, in the epithelial cells, both short and long mRNAs were detected. By using in situ hybridization, expression of the Prox 1 gene was first detected at stage 14 in the early lens placode and slightly preceded the expression of delta 1-crystallin, the first crystallin gene expressed in the developing chicken lens. At later stages of development, Prox 1 mRNA was observed throughout the lens, but it appeared more abundant around the bow region of the equator than in the anterior epithelium or the fibers. In the retina, expression of the Prox 1 gene was detected mainly in the inner nuclear layer during later stages of histogenesis. The conserved pattern of Prox 1/prospero gene expression in vertebrates and Drosophila suggests that Prox 1, like Pax-6, may be essential for eye development in different systematic groups.

Amino Acid Sequence↗
PubMed1998

Activating properties of cocaine and cocaethylene in a behavioral preparation of Drosophila melanogaster.

The use of Drosophila as a model to study the behavioral consequences of stimulant drugs was analyzed in an active preparation of decapitated Drosophila. Application of cocaine and cocaethylene to discrete nerve cord cells regulating motor programs of behavior produced striking patterns of behavioral activity in a concentration-related manner. In general, intense circling behavior and significant wing buzzing activity were distinguishable behavioral markers in flies treated with mM concentrations of cocaine or cocaethylene. The significant changes in motor behavior induced by stimulant drugs in decapitated flies were not reproduced by the application of apomorphine, a direct dopamine (DA) agonist, or octopamine, a naturally occurring transmitter in arthropods. Because both cocaine and cocaethylene interfere with DA reuptake in mammals, we characterized the role of DA receptors mediating increased stereotypy and motor behavior in flies. Coadministration of SCH-23390, a specific D1 receptor antagonist, significantly attenuated the behavior-activating properties of cocaine and cocaethylene in this active experimental preparation. Therefore, the receptor protein mediating the behavioral responses to stimulant drugs in Drosophila is pharmacologically similar to the mammalian D1 subtype. In rats, cocaine- and cocaethylene-induced behavioral activity is complex, with increasing evidence that the D1 receptor interacts significantly with N-methyl-D-aspartate (NMDA) receptor pathways to produce an altered behavioral phenotype. To further characterize additional receptor subtypes targeted by the actions of cocaine and cocaethylene, we pretreated flies with MK-801 and dextromethorphan. Both of these drugs are potent, selective noncompetitive NMDA receptor antagonists. Interestingly, MK-801 and dextromethorphan profoundly reduced the behavior-activating properties of cocaine and cocaethylene in Drosophila. Therefore, as in rats, the NMDA (and D1) receptor pathways in this arthropod represent obligatory targets for the behavioral effects of stimulant drugs.

Adrenergic alpha-Agonists↗
PubMed1998

Dual functions of the heartless fibroblast growth factor receptor in development of the Drosophila embryonic mesoderm.

The Drosophila embryonic mesoderm forms by invagination of the ventral-most blastoderm cells. Subsequent development of this germ layer involves the dorsolateral migration of the internalized cells and expansion by cell division, followed by the specification of particular cell fates through the coordinate actions of both intrinsic and extrinsic regulatory mechanisms. The latter include several intercellular signals that function across germ layers. These processes combine to generate a diversity of mesodermal sub-types, including the cardial and pericardial cells of the heart or dorsal vessel, a complete set of somatic muscle founders each with its unique identity, a population of cells that form the visceral musculature, and other cells that develop into hemocytes and the fat body. Here, we review recent evidence for the involvement of a fibroblast growth factor receptor (FGFR) encoded by the heartless (htl) gene in early directional migration of the Drosophila mesoderm. In addition, we provide new data that 1) demonstrate a second role for Htl in promoting the specification of the precursors to certain cardiac and somatic muscle cells in the Drosophila embryo, independent of its cell migration function, 2) suggest that Ras and at least one other signal transduction pathway act downstream of Htl, and 3) establish a functional relationship between the Ras pathway and Tinman (Tin), a homeodomain factor that is essential for specifying some of the same dorsal mesodermal cells that are dependent on Htl. Finally, parallels between requirements for FGFR signaling in Drosophila and vertebrate mesoderm development are considered.

Animals↗
PubMed1998

In vivo gap repair in Drosophila: a one-way street with many destinations.

While it has long been possible to study the process of recombination in yeast and other single-celled organisms, it has been difficult to distinguish between pathways of meiotic and mitotic recombination in multicellular eukaryotes. The experimental system described here bridges the historically separated fields of Genetic Recombination and DNA Repair in Drosophila. It is now feasible to study the repair of unique double-strand breaks induced in the Drosophila genome by the excision of a P-transposable element or by cleavage at an introduced endonuclease recognition sequence. This repair can be studied in both somatic cells and mitotically dividing germ cells. The repair of these breaks occurs mainly by copying sequence from a template located anywhere in the karyoplasm, and occurs in both male and female flies. This system, which was the first of its kind in metazoan organisms, is now being used for gene targeting in Drosophila. This review summarizes results that provide new insights into the process of gap repair in Drosophila and outline some recent experiments that demonstrate the power of the gene targeting technique.

Animals↗
PubMed1983

Drug metabolizing enzymes in Drosophila melanogaster: teratogenicity of cyclophosphamide in vitro.

This report concerns the attempt to demonstrate the practicability of using microsomal fractions (rat or Drosophila) for activating proteratogens in a Drosophila in vitro teratogen screening assay. Accordingly, a typical proteratogen (cyclophosphamide) was tested before and after microsomal activation and results compared with the drug directly on the in vitro assay. The effects of microsomal activation on known teratogens (thalidomide) and nonteratogens (acetaminophen) were also assayed in order to determine the specificity of the activation process. The results showed activation of the proteratogen into a teratogen occurred as in comparable systems. Activation was specific as teratogens and nonteratogens were not altered in the assay. These preliminary results represent the first direct demonstration that the Drosophila microsomal fraction is capable of bioactivating a proteratogen. This capability further extends the usefulness of the Drosophila embryonic culture assay as an in vitro screen for potential teratogens.

Acetaminophen↗
PubMed2006

Mosquito ribosomal protein S3 lacks a critical glutamine residue associated with DNA repair activity in homologous Drosophila proteins.

In Drosophila melanogaster, ribosomal protein RpS3 has extra-ribosomal activities including apurinic/apyrimidinic lyase activity and N-glycosylase activity that participate in DNA repair. It has been suggested that these activities couple DNA repair to the translational machinery. To establish a basis for participation of RpS3 in DNA repair in mosquitoes, we cloned RpS3 cDNAs from Aedes aegypti and Aedes albopictus mosquito cell lines. The sequence data were used to reconstruct the homologous gene from the Anopheles gambiae database. Mosquito RpS3 is a single copy gene, which in Aedes albopictus, lacks introns in the amino acid coding region. Although RpS3 proteins are well-conserved among eukaryotes, a critical glutamine residue, Q59, essential to robust DNA repair activity in the Drosophila protein, is replaced by an asparagine (N) in all three mosquito RpS3 proteins. In this respect, the mosquito protein resembles human RpS3, which has relatively modest DNA repair activity. None of the insect RpS3 proteins available in the database, other than those from Drosophila, contain glutamine at position 59. However, in the Lepidoptera, N59 is consistently replaced by serine (S), and the putative interactive site at position 134 is replaced by arginine (R). These data suggest that in the case of RpS3, the Drosophila protein may be uniquely unusual in having robust DNA repair activities that are unlikely to be common to RpS3 from other insects.

Aedes↗
PubMed1993

Prospects of using Drosophila for insect neuroendocrine research.

Classical and in vitro approaches for the analysis of the molecular components of neuroendocrine systems often disrupt their close interaction with other bodily systems, which is a crucial aspect of their function in vivo. "Genetic dissection" is an alternative, noninvasive approach which involves the systematic generation of mutations in individual genes, followed by in vivo analysis of the phenotypic effects of altering a single protein at a time avoiding extraneous disruptions. Among insects Drosophila melanogaster is the most suitable model for this approach. This paper explores the application of genetic and molecular techniques available in Drosophila for studying its neuroendocrine system with special emphasis on the production of ecdysone and juvenile hormone. Strategies are described for the generation and identification of endocrine mutations, especially those affecting hormone synthesis and regulation. Once identified by a specific mutation, a gene in Drosophila can be cloned either by chromosomal microdissection and "chromosomal walk" or by transposon tagging. Methods for molecular analysis of the structure and function of a cloned gene and of the protein it encodes are available for further study. Alternatively, a gene can be cloned using heterologous DNA probes or oligonucleotides designed according to the amino acid sequence of a protein. Genes may also be cloned via their pattern of expression (using stage- or tissue-specific cDNA libraries or through transposon-mediated "enhancer detection." Anti-sense RNA, the replacement of the gene by in vitro manipulated versions, or mutagenesis of its endogenous copies can then be used for studying its function in vivo. Information about endocrine genes in Drosophila as well as material such as cloned genes and antibodies should be useful for the analysis of endocrine systems in other insects which are not amenable to genetic manipulations. Such information should be helpful in designing novel means for pest control based on the specific intervention with endocrine systems regulating insect development and reproduction.

Animals↗