NORMAL GENOMIC

• Pueyo JI, Galindo MI, Bishop SA, Couso JP
• Proximal-distal leg development in Drosophila requires the apterous gene and the Lim1 homologue dlim1.
• Development. 2000; 127: 5391-402
• Display abstract

• Proximal-distal leg development in Drosophila involves a battery of genes expressed and required in specific proximal-distal (PD) domains of the appendage. Here we report the characterisation of a new gene of this type, dlim1, a member of the Lhx family of genes whose proteins contain two Lim domains and a homeodomain. We show that the Lhx gene apterous (ap) is also required for PD leg development, and we study the functional interactions between ap, dlim1 and other PD genes during leg development. Our results show that a regulatory network formed by ap and dlim1 plus the homeobox genes aristaless and Bar specifies distal leg cell fates in Drosophila.

• Alatortsev VE, Kovalenko TA, Kalmykova AI
• [Local duplication of genes with insertion of a complex microsatellite]
• Mol Biol (Mosk). 2000; 34: 300-3

• Noll E, Medina M, Hartley D, Zhou J, Perrimon N, Kosik KS
• Presenilin affects arm/beta-catenin localization and function in Drosophila.
• Dev Biol. 2000; 227: 450-64
• Display abstract

• Presenilin is an essential gene for development that when disrupted leads to a neurogenic phenotype that closely resembles Notch loss of function in Drosophila. In humans, many naturally occurring mutations in Presenilin 1 or 2 cause early onset Alzheimer's disease. Both loss of expression and overexpression of Presenilin suggested a role for this protein in the localization of Armadillo/beta-catenin. In blastoderm stage Presenilin mutants, Arm is aberrantly distributed, often in Ubiquitin-immunoreactive cytoplasmic inclusions predominantly located basally in the cell. These inclusions were not observed in loss of function Notch mutants, suggesting that failure to process Notch is not the only consequence of the loss of Presenilin function. Human presenilin 1 expressed in Drosophila produces embryonic phenotypes resembling those associated with mutations in Armadillo and exhibited reduced Armadillo at the plasma membrane that is likely due to retention of Armadillo in a complex with Presenilin. The interaction between Armadillo/beta-catenin and Presenilin 1 requires a third protein which may be delta-catenin. Our results suggest that Presenilin may regulate the delivery of a multiprotein complex that regulates Armadillo trafficking between the adherens junction and the proteasome.

• Yu F, Morin X, Cai Y, Yang X, Chia W
• Analysis of partner of inscuteable, a novel player of Drosophila asymmetric divisions, reveals two distinct steps in inscuteable apical localization.
• Cell. 2000; 100: 399-409
• Display abstract

• Asymmetric localization is a prerequisite for inscuteable (insc) to function in coordinating and mediating asymmetric cell divisions in Drosophila. We show here that Partner of Inscuteable (Pins), a new component of asymmetric divisions, is required for Inscuteable to asymmetrically localize. In the absence of pins, Inscuteable becomes cytoplasmic and asymmetric divisions of neuroblasts and mitotic domain 9 cells show defects reminiscent of insc mutants. Pins colocalizes with Insc and interacts with the region necessary and sufficient for directing its asymmetric localization. Analyses of pins function in neuroblasts reveal two distinct steps for Insc apical cortical localization: A pins-independent, bazooka-dependent initiation step during delamination (interphase) and a later maintenance step during which Baz, Pins, and Insc localization are interdependent.

• Stowers RS, Russell S, Garza D
• The 82F late puff contains the L82 gene, an essential member of a novel gene family.
• Dev Biol. 1999; 213: 116-30
• Display abstract

• Metamorphosis in Drosophila results from a hierarchy of ecdysone-induced gene expression initiated at the end of the third larval instar. A now classical model of this hierarchy was proposed based on observations of the activity of polytene chromosome "puffs" which distinguished "early" puffs as those directly induced by ecdysone and "late" puffs as those which become active as a secondary response to the hormone. We report here the isolation and characterization of the L82 gene corresponding to the extensively characterized late puff at 82F. L82 is a complex gene that spans at least 50 kb of genomic DNA, produces at least seven different nested mRNAs, and has homology to a novel gene family. In contrast to most previously characterized puff genes, the broad developmental expression pattern of L82 suggests that it is controlled by both ecdysone-dependent and ecdysone-independent regulatory mechanisms. L82 mutations were identified by transgene rescue of developmental delay and eclosion lethal phenotypes.

• Sedkov Y et al.
• Molecular genetic analysis of the Drosophila trithorax-related gene which encodes a novel SET domain protein.
• Mech Dev. 1999; 82: 171-9
• Display abstract

• The products of the trithorax and Polycomb groups genes maintain the activity and silence, respectively, of many developmental genes including genes of the homeotic complexes. This transcriptional regulation is likely to involve modification of chromatin structure. Here, we report the cloning and characterization of a new gene, trithorax-related (trr), which shares sequence similarities with members of both the trithorax and Polycomb groups. The trr transcript is 9.6 kb in length and is present throughout development. The TRR protein, as predicted from the nucleotide sequence of the open reading frame, is 2431 amino acids in length and contains a PHD finger-like domain and a SET domain, two highly conserved protein motifs found in several trithorax and Polycomb group proteins, and in modifiers of position effect variegation. TRR is most similar in sequence to the human ALR protein, suggesting that trr is a Drosophila homologue of the ALR. TRR is also highly homologous to Drosophila TRITHORAX protein and to its human homologue, ALL-1/HRX. However, preliminary genetic analysis of a trr null allele suggests that TRR protein may not be involved in regulation of homeotic genes (i.e. not a member of the trithorax or Polycomb groups) or in position effect variegation.

• Okuda T et al.
• Molecular cloning of macrophin, a human homologue of Drosophila kakapo with a close structural similarity to plectin and dystrophin.
• Biochem Biophys Res Commun. 1999; 264: 568-74
• Display abstract

• We have determined the complete cDNA coding sequence of a novel cytoskeletal protein by the degenerative primer-mediated PCR strategy. This novel gene, named as macrophin (microfilament and actin filament cross-linker protein related to plectin and dystrophin, Accession No. AB029290), appears to be a human homologue of a Drosophila gene, kakapo, and shows close similarity to plectin and dystrophin on the search of BLAST homology-computed database. Comparison of the deduced protein sequences for macrophin and kakapo revealed that they were 66% similar, and both of them have an NH2-terminal actin-binding domain, a central rod region composed of spectrin-like repeats, and COOH-terminal Gas2-related region. The predicted sequences for macrophin are 5430 amino acids in length with a calculated molecular mass of 620 kDa, which is one of the largest size idenfied in human cytoskeletal proteins. High expression of macrophin was observed in brain, heart, lung, placenta, liver, kidney, and pancreas. In pancreas, we found that macrophin was specifically expressed in acinar cells than islet cells by in situ hybridization. By using radiation hybrid panel, we have mapped the macrophin gene to the chromosome 1p31-32.

• Bray S
• DPP on the brinker.
• Trends Genet. 1999; 15: 140-140

• Curtin KD, Zhang Z, Wyman RJ
• Drosophila has several genes for gap junction proteins.
• Gene. 1999; 232: 191-201
• Display abstract

• The Innexin gene family forms gap junctions in invertebrates. Many genes in this family have been identified in Caenorhabditis elegans, but only two in Drosophila. We have used PCR techniques to identify three new members of this family from Drosophila. These are designated pas-related proteins (prp) 6, 7, and 33. The putative proteins coded by these new genes show 25-35% identity and 39-66% similarity to other Drosophila innexins and share a similar hydrophobicity profile. The genes form two small clusters on the X-chromosome, with three of the genes sitting within 10kb of each other. The closeness in sequence and location suggests an evolutionary origin of these genes via local duplication. In situ hybridization shows expression in the CNS, gut and epidermis. Each gene has a distinct pattern of expression in different tissues at different developmental times. However, parts of the expression patterns overlap, especially for prp33 and ogre which may be expressed from the same transcriptional enhancers. This suggest that the Prp33 and Ogre proteins may join in forming heteromeric gap junction channels.

• Hatzfeld M
• The armadillo family of structural proteins.
• Int Rev Cytol. 1999; 186: 179-224
• Display abstract

• The armadillo gene is a segment polarity gene of Drosophila involved in signal transduction through wingless. Since the mid-1980s, a growing number of related proteins have been identified based on sequence homologies. These proteins share a central domain that is composed of a series of imperfect 45 amino acid repeats. Armadillo family members reveal diverse cellular locations reflecting their diverse functions. A single protein exerts several functions through interactions of its armadillo repeat domain with diverse binding partners. The proteins combine structural roles as cell-contact and cytoskeleton-associated proteins and signaling functions by generating and transducing signals affecting gene expression. The study of armadillo family members has made it increasingly clear that a distinction between structural proteins on the one hand and signaling molecules on the other is rather artificial. Instead armadillo family members exert both functions by interacting with a number of distinct cellular-binding partners.

• Sato A, Kojima T, Ui-Tei K, Miyata Y, Saigo K
• Dfrizzled-3, a new Drosophila Wnt receptor, acting as an attenuator of Wingless signaling in wingless hypomorphic mutants.
• Development. 1999; 126: 4421-30
• Display abstract

• In Drosophila, two Frizzled proteins, Frizzled and Dfrizzled-2, have been reported to serve as receptors of Wingless. Here, we identified the third member of the Drosophila Frizzled family (Dfrizzled-3). In contrast to Dfrizzled-2, Dfrizzled-3 was transcriptionally upregulated by Wingless signaling. Although Dfrizzled-3 was capable of binding to Wingless in vitro, Wingless-dependent Armadillo/beta -catenin stabilization occurred much less effectively in Drosophila cells transfected with Dfrizzled-3 than in those with Dfrizzled-2. Flies lacking Dfrizzled-3 activity were viable and fertile, with few morphological defects. Genetic and immunochemical analysis indicated that the absence of Dfrizzled-3 activity suppresses the effects of hypomorphic wingless mutations such as failure of wing and antenna formation and restores target gene expression to the normal levels without change in wingless expression. Wingless signaling may thus be attenuated by Dfrizzled-3 at least in wingless hypomorphic mutants.

• Marquart J, Alexief-Damianof C, Preiss A, Maier D
• Rapid divergence in the course of Drosophila evolution reveals structural important domains of the Notch antagonist Hairless.
• Dev Genes Evol. 1999; 209: 155-64
• Display abstract

• Hairless is a member of the Notch signalling pathway, where it acts as antagonist by binding to Suppressor of Hairless [Su(H)], thereby inhibiting Notch target gene activation. The pathway and its members are highly conserved in metazoans from worms to humans. However, a Hairless orthologue from another species has not yet been identified. The identification of Hairless in largely diverged species by cross-hybridization has failed so far probably due to a low degree of conservation. Therefore, we turned to D. hydei where a Hairless mutation has been described before. The D. hydei Hairless orthologue is reasonably well conserved with regard to gene structure and expression. The prospective Hairless protein orthologues share several highly conserved regions which are separated by quite diverged stretches. As to be expected, the largest region of high conservation corresponds to the Su(H) binding domain. This region is also functionally conserved, since this D. hydei protein domain binds very strongly to the D. melanogaster Su(H) protein. The other conserved regions support our earlier structure-function analysis since they nicely correspond to previously defined, functionally important protein domains. Most notably, the very C-terminal domain which is very sensitive to structural alterations, is nearly identical between the two species. In summary, this evolutionary study improves the knowledge on functionally significant domains of the Hairless protein, and may be helpful for the future identification of homologues in other animals, especially in vertebrates.

• Barry MK, Triplett AA, Christensen AC
• A peritrophin-like protein expressed in the embryonic tracheae of Drosophila melanogaster.
• Insect Biochem Mol Biol. 1999; 29: 319-27
• Display abstract

• We have cloned and sequenced a cDNA from Drosophila melanogaster that encodes a protein homologous to the peritrophins, a family of chitin-binding proteins from the peritrophic matrix of insects. Unexpectedly, the gene, Gasp, is expressed in the embryonic tracheae. We suggest that this family of proteins may be present in other tissues than the peritrophic matrix, particularly where nutrient or gas exchange are important, and/or where invasion by parasites or viruses is possible. We have also mapped two similar genes that had been sequenced by the Berkeley Drosophila Genome Project, and find that these three very similar genes are not clustered, but are located on three different chromosomes.

• Ruhf ML, Meister M
• The Drosophila homologue of ribosomal protein L8.
• Insect Biochem Mol Biol. 1999; 29: 349-53
• Display abstract

• We have cloned the gene encoding the Drosophila melanogaster homologue of ribosomal protein L8. It contains two introns: one in the 5' untranslated region and the second in the beginning of the ORF, and encodes a 256-residue protein which is highly conserved when compared with RpL8 proteins of other organisms. The gene is present as a single copy in the Drosophila genome and maps at position 62E6-7 on polytene chromosomes. It is expressed ubiquitously at all stages of development. It is located close to the gene encoding RpL12 and both are candidate targets of the Minute mutation, M(3)LS2, mapped in the region 62E-63A.

• Inohara N, Nunez G
• Genes with homology to DFF/CIDEs found in Drosophila melanogaster.
• Cell Death Differ. 1999; 6: 823-4

• Xu X, Yin Z, Hudson JB, Ferguson EL, Frasch M
• Smad proteins act in combination with synergistic and antagonistic regulators to target Dpp responses to the Drosophila mesoderm.
• Genes Dev. 1998; 12: 2354-70
• Display abstract

• Dorsal mesoderm induction in arthropods and ventral mesoderm induction in vertebrates are closely related processes that involve signals of the BMP family. In Drosophila, induction of visceral mesoderm, dorsal muscles, and the heart by Dpp is, at least in part, effected through the transcriptional activation and function of the homeobox gene tinman in dorsal mesodermal cells during early embryogenesis. Here we present a functional dissection of a tinman enhancer that mediates the Dpp response. We provide evidence that mesoderm-specific induction of tinman requires the binding of both activators and repressors. Screens for binding factors yielded Tinman itself and the Smad4 homolog Medea. We show that the binding and synergistic activities of Smad and Tinman proteins are critical for mesodermal tinman induction, whereas repressor binding sites prevent induction in the dorsal ectoderm and amnioserosa. Thus, integration of positive and negative regulators on enhancers of target genes appears to be an important mechanism in tissue-specific induction by TGF-beta molecules.

• Prokop A, Uhler J, Roote J, Bate M
• The kakapo mutation affects terminal arborization and central dendritic sprouting of Drosophila motorneurons.
• J Cell Biol. 1998; 143: 1283-94
• Display abstract

• The lethal mutation l(2)CA4 causes specific defects in local growth of neuronal processes. We uncovered four alleles of l(2)CA4 and mapped it to bands 50A-C on the polytene chromosomes and found it to be allelic to kakapo (. Genetics. 146:275- 285). In embryos carrying our kakapo mutant alleles, motorneurons form correct nerve branches, showing that long distance growth of neuronal processes is unaffected. However, neuromuscular junctions (NMJs) fail to form normal local arbors on their target muscles and are significantly reduced in size. In agreement with this finding, antibodies against kakapo (Gregory and Brown. 1998. J. Cell Biol. 143:1271-1282) detect a specific epitope at all or most Drosophila NMJs. Within the central nervous system of kakapo mutant embryos, neuronal dendrites of the RP3 motorneuron form at correct positions, but are significantly reduced in size. At the subcellular level we demonstrate two phenotypes potentially responsible for the defects in neuronal branching: first, transmembrane proteins, which can play important roles in neuronal growth regulation, are incorrectly localized along neuronal processes. Second, microtubules play an important role in neuronal growth, and kakapo appears to be required for their organization in certain ectodermal cells: On the one hand, kakapo mutant embryos exhibit impaired microtubule organization within epidermal cells leading to detachment of muscles from the cuticle. On the other, a specific type of sensory neuron (scolopidial neurons) shows defects in microtubule organization and detaches from its support cells.

• Wasserman S
• FH proteins as cytoskeletal organizers.
• Trends Cell Biol. 1998; 8: 111-5
• Display abstract

• Regulation of cell shape is a poorly understood yet central issue in cell biology. Recent experiments indicate that FH proteins link cellular signalling pathways to changes in cell shape. Members of the FH protein family play essential roles in cytokinesis and in driving alterations in cell polarity. This review discusses the structure and function of these proteins and examines the evidence that they interact specifically with Rho GTPases and profilin to organize the actin-based cytoskeleton.

• Martin-Blanco E et al.
• puckered encodes a phosphatase that mediates a feedback loop regulating JNK activity during dorsal closure in Drosophila.
• Genes Dev. 1998; 12: 557-70
• Display abstract

• The activation of MAPKs is controlled by the balance between MAPK kinase and MAPK phosphatase activities. The latter is mediated by a subset of phosphatases with dual specificity (VH-1 family). Here, we describe a new member of this family encoded by the puckered gene of Drosophila. Mutations in this gene lead to cytoskeletal defects that result in a failure in dorsal closure related to those associated with mutations in basket, the Drosophila JNK homolog. We show that puckered mutations result in the hyperactivation of DJNK, and that overexpression of puc mimics basket mutant phenotypes. We also show that puckered expression is itself a consequence of the activity of the JNK pathway and that during dorsal closure, JNK signaling has a dual role: to activate an effector, encoded by decapentaplegic, and an element of negative feedback regulation encoded by puckered.

• Lin SC, Lin MH, Horvath P, Reddy KL, Storti RV
• PDP1, a novel Drosophila PAR domain bZIP transcription factor expressed in developing mesoderm, endoderm and ectoderm, is a transcriptional regulator of somatic muscle genes.
• Development. 1997; 124: 4685-96
• Display abstract

• In vertebrates, transcriptional control of skeletal muscle genes during differentiation is regulated by enhancers that direct the combinatorial binding and/or interaction of MEF2 and the bHLH MyoD family of myogenic factors. We have shown that Drosophila MEF2 plays a role similar to its vertebrate counterpart in the regulation of the Tropomyosin I gene in the development of Drosophila somatic muscles, however, unlike vertebrates, Drosophila MEF2 interacts with a muscle activator region that does not have binding sites for myogenic bHLH-like factors or any other known Drosophila transcription factors. We describe here the isolation and characterization of a component of the muscle activator region that we have named PDP1 (PAR domain protein 1). PDP1 is a novel transcription factor that is highly homologous to the PAR subfamily of mammalian bZIP transcription factors HLF, DBP and VBP/TEF. This is the first member of the PAR subfamily of bZIP transcription factors to be identified in Drosophila. We show that PDP1 is involved in regulating expression of the Tropomyosin I gene in somatic body-wall and pharyngeal muscles by binding to DNA sequences within the muscle activator that are required for activator function. Mutations that eliminate PDP1 binding eliminate muscle activator function and severely reduce expression of a muscle activator plus MEF2 mini-enhancer. These and previous results suggest that PDP1 may function as part of a larger protein/DNA complex that interacts with MEF2 to regulate transcription of Drosophila muscle genes. Furthermore, in addition to being expressed in the mesoderm that gives rise to the somatic muscles, PDP1 is also expressed in the mesodermal fat body, the developing midgut endoderm, the hindgut and Malpighian tubules, and the epidermis and central nervous system, suggesting that PDP1 is also involved in the terminal differentiation of these tissues.

• Endo K, Matsuda Y, Kobayashi S
• Mdes, a mouse homolog of the Drosophila degenerative spermatocyte gene is expressed during mouse spermatogenesis.
• Dev Growth Differ. 1997; 39: 399-403
• Display abstract

• A new mouse gene Mdes has been identified, which has a significant sequence homology with a Drosophila gene degenerative spermatocyte (des) that is required for the initiation of meiosis in spermatogenesis. The expression pattern of the Mdes transcript during mouse spermatogenesis is similar to that of the des transcript curing Drosophila spermatogenesis. Based on these results, it is proposed that the products of Mdes and des have a phylogenetically conserved role in vertebrate and invertebrate spermatogenesis.

• Cunniff J, Chiu YH, Morris NR, Warrior R
• Characterization of DnudC, the Drosophila homolog of an Aspergillus gene that functions in nuclear motility.
• Mech Dev. 1997; 66: 55-68
• Display abstract

• Nuclear migration plays a prominent role in a broad range of developmental processes. We have cloned a Drosophila gene, DnudC, encoding a protein that is evolutionarily conserved between humans and fungi. The Aspergillus homolog, nudC, is one of a group of genes required for nuclear migration. DnudC encodes a 38.5-kDa protein, and the carboxy terminal half of the protein shares 52% amino acid identity with Aspergillus nudC. We show that the structural homology between DnudC and nudC extends to the functional level since the Drosophila gene can rescue the nuclear migration defects seen in Aspergillus nudC mutants. Immunolocalization studies using antisera against DnudC reveal that the protein is localized to the cytoplasm in Drosophila ovaries and embryos. Our data suggest that the nudC genes may be components of a functionally conserved pathway involved in the regulation of nuclear motility.

• Ruiz-Gomez M, Romani S, Hartmann C, Jackle H, Bate M
• Specific muscle identities are regulated by Kruppel during Drosophila embryogenesis.
• Development. 1997; 124: 3407-14
• Display abstract

• During Drosophila embryogenesis, mesodermal cells are recruited to form a complex pattern of larval muscles. The formation of the pattern is initiated by the segregation of a special class of founder myoblasts. Single founders fuse with neighbouring nonfounder myoblasts to form the precursors of individual muscles. Founders and the muscles that they give rise to have specific patterns of gene expression and it has been suggested that it is the expression of these founder cell genes that determines individual muscle attributes such as size, shape, insertion sites and innervation. We find that the segmentation gene Kruppel is expressed in a subset of founders and muscles, regulates specific patterns of gene expression in these cells and is required for the acquisition of proper muscle identity. We show that gain and loss of Kruppel expression in sibling founder cells is sufficient to switch these cells, and the muscles that they give rise to, between alternative cell fates.

• Gautier P, Ledent V, Massaer M, Dambly-Chaudiere C, Ghysen A
• tap, a Drosophila bHLH gene expressed in chemosensory organs.
• Gene. 1997; 191: 15-21
• Display abstract

• We have isolated a Drosophila bHLH gene, tap, that is expressed in a small subset of neurons when they undergo differentiation. In the peripheral nervous system, tap is expressed exclusively in one of the neurons that innervate each larval chemosensory organ, possibly controlling the specific properties of that neuron. Sequence comparisons suggest that tap is most closely related to two bHLH genes identified in several vertebrate species, neurogenin and neuroD, which are involved respectively in neural determination and in neuronal differentiation.

• Rosenberg-Hasson Y, Renert-Pasca M, Volk T
• A Drosophila dystrophin-related protein, MSP-300, is required for embryonic muscle morphogenesis.
• Mech Dev. 1996; 60: 83-94
• Display abstract

• Proteins from the spectrin superfamily contribute to cell polarity and shape during the morphogenetic that accompany embryogenesis. Drosophila MSP-300, a member of the spectrin superfamily, is expressed in somatic, visceral and heart embryonic muscles. Cloning and sequence analysis of various spliced forms of MSP-300 reveals functional and structural similarities between MSP-300 and vertebrate Dystrophin, the product of the Duchenne Muscular Dystrophy gene. The identification of a strain mutant for the MSP-300 gene is described. Analysis of the somatic muscle phenotype in MSP-300 mutant embryos suggests that the protein contributes to the integrity of the somatic and visceral muscle during periods of significant morphogenetic change. Functional synergism between MSP-300 and laminin is demonstrated by the analysis of the phenotype of embryos mutant for both genes. The enhancement of aberrant muscle phenotype in the double mutants suggests a link between MSP-300 and laminin function in mediating proper extension of the myotube towards the epidermal muscle attachment site. In addition, both genes function to establish gut integrity. In view of the functional and structural similarities between MSP-300 and Dystrophin, it is postulated that Dystrophin is not only required for proper muscle function in adult life but also contributes to muscle morphogenesis during the development of the vertebrate embryo.

• Gross CT, McGinnis W
• DEAF-1, a novel protein that binds an essential region in a Deformed response element.
• EMBO J. 1996; 15: 1961-70
• Display abstract

• A 120 bp homeotic response element that is regulated specifically by Deformed in Drosophila embryos contains a single binding site for Deformed protein. However, a 24 bp sub-element containing this site does not constitute a Deformed response element. Specific activation requires a second region in the 120 bp element, which presumably contains one or more binding sites for Deformed cofactors. We have isolated a novel protein from Drosophila nuclear extracts which binds specifically to a site in this second region. This protein, which we call DEAF-1 (Deformed epidermal autoregulatory factor-1), contains three conserved domains. One of these includes a cysteine repeat motif that is similar to a motif found in Drosophila Nervy and the human MTG8 proto-oncoprotein, and another matches a region of Drosophila Trithorax. Mutations in the response element designed to improve binding to DEAF-1 in vitro resulted in increased embryonic expression. Conversely, small mutations designed to diminish binding to DEAF-1 resulted in reduced expression of the element. Thus, DEAF-1 is likely to contribute to the functional activity, and perhaps to the homeotic specificity, of this response element. Consistent with this hypothesis, we have discovered DEAF-1 binding sites in other Deformed response elements.

• Goubeaud A, Knirr S, Renkawitz-Pohl R, Paululat A
• The Drosophila gene alien is expressed in the muscle attachment sites during embryogenesis and encodes a protein highly conserved between plants, Drosophila and vertebrates.
• Mech Dev. 1996; 57: 59-68
• Display abstract

• We have found a novel gene (alien) that is expressed exclusively in the muscle attachment sites (apodemes) during embryogenesis in Drosophila. Antibodies raised against the Alien protein enable us to follow the developing attachments from state 11/12 until stage 16/17. The coding region of the Drosophila alien gene is highly conserved to a gene of unknown function, isolated from a plant (Loo et at., 1995), and to the human TRIP15 gene (Lee et al., 1995). Searching for thyroid receptor interacting proteins, TRIP15 was isolated as a negative regulator. Whether there is a functional correlation to Alien remains to be analyzed. Alien expression is independent of muscle formation, as shown in rolling stone mutant embryos. Even in twist and snail mutants, lacking mesodermal development, alien expression is fairly normal, showing a rather autonomous development of the apodemes. The conservation of alien suggests an important role in differentiation.

• Norris AL et al.
• Characterization of the human beta-catenin gene.
• Mamm Genome. 1996; 7: 160-2

• Burglin TR
• Warthog and groundhog, novel families related to hedgehog.
• Curr Biol. 1996; 6: 1047-50