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1.
Development ; 150(18)2023 09 15.
Artigo em Inglês | MEDLINE | ID: mdl-37681291

RESUMO

Vertebrate podocytes and Drosophila nephrocytes display slit diaphragms, specialised cell junctions that are essential for the execution of the basic excretory function of ultrafiltration. To elucidate the mechanisms of slit diaphragm assembly we have studied their formation in Drosophila embryonic garland nephrocytes. These cells of mesenchymal origin lack overt apical-basal polarity. We find that their initial membrane symmetry is broken by an acytokinetic cell division that generates PIP2-enriched domains at their equator. The PIP2-enriched equatorial cortex becomes a favourable domain for hosting slit diaphragm proteins and the assembly of the first slit diaphragms. Indeed, when this division is either prevented or forced to complete cytokinesis, the formation of diaphragms is delayed to larval stages. Furthermore, although apical polarity determinants also accumulate at the equatorial cortex, they do not appear to participate in the recruitment of slit diaphragm proteins. The mechanisms we describe allow the acquisition of functional nephrocytes in embryos, which may confer on them a biological advantage similar to the formation of the first vertebrate kidney, the pronephros.


Assuntos
Citocinese , Drosophila , Animais , Divisão Celular , Córtex Cerebral , Diafragma
2.
Development ; 150(10)2023 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-37213082
3.
PLoS Genet ; 11(8): e1005463, 2015 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-26305360

RESUMO

During development, proper differentiation and final organ size rely on the control of territorial specification and cell proliferation. Although many regulators of these processes have been identified, how both are coordinated remains largely unknown. The homeodomain Iroquois/Irx proteins play a key, evolutionarily conserved, role in territorial specification. Here we show that in the imaginal discs, reduced function of Iroquois genes promotes cell proliferation by accelerating the G1 to S transition. Conversely, their increased expression causes cell-cycle arrest, down-regulating the activity of the Cyclin E/Cdk2 complex. We demonstrate that physical interaction of the Iroquois protein Caupolican with Cyclin E-containing protein complexes, through its IRO box and Cyclin-binding domains, underlies its activity in cell-cycle control. Thus, Drosophila Iroquois proteins are able to regulate cell-autonomously the growth of the territories they specify. Moreover, our results provide a molecular mechanism for a role of Iroquois/Irx genes as tumour suppressors.


Assuntos
Proteínas de Drosophila/fisiologia , Proteínas de Homeodomínio/fisiologia , Animais , Ciclo Celular , Linhagem Celular , Proliferação de Células , Olho Composto de Artrópodes/citologia , Olho Composto de Artrópodes/metabolismo , Ciclina E/metabolismo , Quinase 2 Dependente de Ciclina/metabolismo , Proteínas de Drosophila/metabolismo , Drosophila melanogaster , Discos Imaginais/citologia , Discos Imaginais/metabolismo , Ligação Proteica , Mapas de Interação de Proteínas
4.
Fly (Austin) ; 9(3): 126-31, 2015.
Artigo em Inglês | MEDLINE | ID: mdl-26760760

RESUMO

Drosophila Iroquois (Iro) proteins are components of the TALE homeodomain family of transcriptional regulators. They play key roles in territorial specification and pattern formation. A recent study has disclosed a novel developmental function of the Iro proteins. In the eye and wing imaginal discs, they can regulate the size of the territories that they specify. They do so by cell-autonomously controlling cell cycle progression. Indeed, Iro proteins down-regulate the activity of the CyclinE/Cdk2 complex by a transcription-independent mechanism. This novel function is executed mainly through 2 evolutionarily conserved domains of the Iro proteins: the Cyclin Binding Domain and the IRO-box, which mediate their binding to CyclinE-containing protein complexes. Here we discuss the functional implications of the control of the cell cycle by Iro proteins for development and oncogenesis.


Assuntos
Ciclo Celular/genética , Proteínas de Drosophila/fisiologia , Drosophila/citologia , Proteínas de Homeodomínio/fisiologia , Sequência de Aminoácidos , Animais , Sítios de Ligação , Sequência Conservada , Ciclina E/genética , Ciclina E/metabolismo , Quinase 2 Dependente de Ciclina/genética , Quinase 2 Dependente de Ciclina/metabolismo , Regulação para Baixo , Drosophila/crescimento & desenvolvimento , Drosophila/metabolismo , Proteínas de Drosophila/genética , Proteínas de Drosophila/metabolismo , Proteínas de Homeodomínio/genética , Proteínas de Homeodomínio/metabolismo , Domínios Proteicos , Alinhamento de Sequência
5.
Fly (Austin) ; 6(4): 234-9, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-22878648

RESUMO

Dorsoventral (DV) axis formation in Drosophila begins during oogenesis through the graded activation of the EGF receptor (EGFR)-Ras-MAPK signaling pathway in the follicle cell layer of the egg chamber. EGFR signaling, which is higher in dorsal follicle cells, represses expression of the sulfotransferase-encoding gene pipe, thereby delimiting a ventral domain of Pipe activity that is critical for the subsequent induction of ventral embryonic fates. We have characterized the transcriptional circuit that links EGFR signaling to pipe repression: in dorsal follicle cells, the homeodomain transcription factor Mirror (Mirr), which is induced by EGFR signaling, directly represses pipe transcription, whereas in ventral follicle cells, the HMG-box protein Capicua (Cic) supports pipe expression by repressing mirr. Although Cic is under negative post-transcriptional regulation by Ras-MAPK signaling in different contexts, the relevance of this mechanism for the interpretation of the EGFR signal during DV pattern formation remains unclear. Here, we consider a model where EGFR-mediated downregulation of Cic modulates the spatial distribution of Mirr protein in lateral follicle cells, thereby contributing to define the position at which the pipe expression border is formed.


Assuntos
Padronização Corporal/genética , Regulação para Baixo , Proteínas de Drosophila/genética , Proteínas de Drosophila/fisiologia , Drosophila/citologia , Receptores ErbB/fisiologia , Proteínas HMGB/genética , Receptores de Peptídeos de Invertebrados/fisiologia , Proteínas Repressoras/genética , Animais , Drosophila/genética , Drosophila/metabolismo , Proteínas de Drosophila/metabolismo , Embrião não Mamífero/citologia , Embrião não Mamífero/metabolismo , Regulação da Expressão Gênica no Desenvolvimento , Proteínas HMGB/metabolismo , Proteínas HMGB/fisiologia , Modelos Biológicos , Proteínas Repressoras/metabolismo , Proteínas Repressoras/fisiologia , Transdução de Sinais , Sulfotransferases/genética , Sulfotransferases/metabolismo
6.
Development ; 139(6): 1110-4, 2012 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-22318229

RESUMO

Dorsoventral (DV) axis formation in Drosophila begins with selective activation of EGFR, a receptor tyrosine kinase (RTK), in dorsal-anterior (DA) ovarian follicle cells. A critical event regulated by EGFR signaling is the repression of the sulfotransferase-encoding gene pipe in dorsal follicle cells, but how this occurs remains unclear. Here we show that Mirror (Mirr), a homeodomain transcription factor induced by EGFR signaling in DA follicle cells, directly represses pipe expression by binding to a conserved element in the pipe regulatory region. In addition, we find that the HMG-box protein Capicua (Cic) supports pipe expression in ventral follicle cells by repressing Mirr in this region. Interestingly, this role of Cic resembles its function in regulating anteroposterior (AP) body patterning, where Cic supports gap gene expression in central regions of the embryo by repressing Tailless, a repressor induced by RTK signaling at the embryonic poles. Thus, related RTK-Cic repressor circuits regulate the early stages of Drosophila DV and AP body axis formation.


Assuntos
Padronização Corporal/genética , Proteínas de Drosophila/genética , Proteínas de Drosophila/metabolismo , Drosophila melanogaster/embriologia , Receptores ErbB/metabolismo , Proteínas do Olho/metabolismo , Regulação da Expressão Gênica no Desenvolvimento , Proteínas HMGB/metabolismo , Proteínas de Homeodomínio/metabolismo , Receptores de Peptídeos de Invertebrados/metabolismo , Proteínas Repressoras/metabolismo , Sulfotransferases/genética , Sulfotransferases/metabolismo , Fatores de Transcrição/metabolismo , Animais , Sequência Conservada , Proteínas de Drosophila/biossíntese , Drosophila melanogaster/citologia , Drosophila melanogaster/genética , Drosophila melanogaster/metabolismo , Embrião não Mamífero/metabolismo , Feminino , Folículo Ovariano/citologia , Folículo Ovariano/embriologia , Folículo Ovariano/metabolismo , Sequências Reguladoras de Ácido Nucleico , Transdução de Sinais , Sulfotransferases/biossíntese
7.
Genome Res ; 22(4): 642-55, 2012 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-22234889

RESUMO

Developmental genes are regulated by complex, distantly located cis-regulatory modules (CRMs), often forming genomic regulatory blocks (GRBs) that are conserved among vertebrates and among insects. We have investigated GRBs associated with Iroquois homeobox genes in 39 metazoans. Despite 600 million years of independent evolution, Iroquois genes are linked to ankyrin-repeat-containing Sowah genes in nearly all studied bilaterians. We show that Iroquois-specific CRMs populate the Sowah locus, suggesting that regulatory constraints underlie the maintenance of the Iroquois-Sowah syntenic block. Surprisingly, tetrapod Sowah orthologs are intronless and not associated with Iroquois; however, teleost and elephant shark data demonstrate that this is a derived feature, and that many Iroquois-CRMs were ancestrally located within Sowah introns. Retroposition, gene, and genome duplication have allowed selective elimination of Sowah exons from the Iroquois regulatory landscape while keeping associated CRMs, resulting in large associated gene deserts. These results highlight the importance of CRMs in imposing constraints to genome architecture, even across large phylogenetic distances, and of gene duplication-mediated genetic redundancy to disentangle these constraints, increasing genomic plasticity.


Assuntos
Genoma/genética , Proteínas de Homeodomínio/genética , Invertebrados/genética , Vertebrados/genética , Sequência de Aminoácidos , Animais , Evolução Molecular , Duplicação Gênica/genética , Regulação da Expressão Gênica no Desenvolvimento , Genômica/métodos , Proteínas de Homeodomínio/classificação , Insetos/classificação , Insetos/embriologia , Insetos/genética , Invertebrados/classificação , Invertebrados/embriologia , Dados de Sequência Molecular , Filogenia , Retroelementos/genética , Homologia de Sequência de Aminoácidos , Especificidade da Espécie , Vertebrados/classificação , Vertebrados/embriologia
8.
PLoS Genet ; 7(7): e1002186, 2011 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-21811416

RESUMO

A central issue of myogenesis is the acquisition of identity by individual muscles. In Drosophila, at the time muscle progenitors are singled out, they already express unique combinations of muscle identity genes. This muscle code results from the integration of positional and temporal signalling inputs. Here we identify, by means of loss-of-function and ectopic expression approaches, the Iroquois Complex homeobox genes araucan and caupolican as novel muscle identity genes that confer lateral transverse muscle identity. The acquisition of this fate requires that Araucan/Caupolican repress other muscle identity genes such as slouch and vestigial. In addition, we show that Caupolican-dependent slouch expression depends on the activation state of the Ras/Mitogen Activated Protein Kinase cascade. This provides a comprehensive insight into the way Iroquois genes integrate in muscle progenitors, signalling inputs that modulate gene expression and protein activity.


Assuntos
Proteínas de Drosophila/genética , Drosophila melanogaster/genética , Proteínas de Homeodomínio/genética , Músculos/metabolismo , Fatores de Transcrição/genética , Animais , Animais Geneticamente Modificados , Sequência de Bases , Linhagem Celular , Proteínas de Drosophila/metabolismo , Drosophila melanogaster/citologia , Drosophila melanogaster/embriologia , Embrião não Mamífero/embriologia , Embrião não Mamífero/metabolismo , Regulação da Expressão Gênica no Desenvolvimento , Proteínas de Homeodomínio/metabolismo , Hibridização In Situ , Microscopia Confocal , Proteínas Quinases Ativadas por Mitógeno/metabolismo , Desenvolvimento Muscular/genética , Músculos/embriologia , Proteínas Nucleares/genética , Proteínas Nucleares/metabolismo , Homologia de Sequência do Ácido Nucleico , Transdução de Sinais/genética , Fatores de Transcrição/metabolismo , Proteínas ras/metabolismo
9.
J Cell Sci ; 124(Pt 2): 240-51, 2011 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-21172808

RESUMO

Many epithelial tissues undergo extensive remodelling during morphogenesis. How their epithelial features, such as apicobasal polarity or adhesion, are maintained and remodelled and how adhesion and polarity proteins contribute to morphogenesis are two important questions in development. Here, we approach these issues by investigating the role of the apical determinant protein Crumbs (Crb) during the morphogenesis of the embryonic Drosophila tracheal system. Crb accumulates differentially throughout tracheal development and is required for different tracheal events. The earliest requirement for Crb is for tracheal invagination, which is preceded by an enhanced accumulation of Crb in the invagination domain. There, Crb, acting in parallel with the epidermal growth factor receptor (Egfr) pathway, is required for tracheal cell apical constriction and for organising an actomyosin complex, which we propose is mediated by Crb recruitment of moesin (Moe). The ability of a Crb isoform unable to rescue polarity in crb mutants to otherwise rescue their invagination phenotype, and the converse inability of a FERM-binding domain mutant Crb to rescue faulty invagination, support our hypothesis that it is the absence of Crb-dependent Moe enrichment, and not the polarity defect, that mainly underlies the crb invagination phenotype. This hypothesis is supported by the phenotype of lethal giant larvae (lgl); crb double mutants. These results unveil a link between Crb and the organisation of the actin cytoskeleton during morphogenesis.


Assuntos
Polaridade Celular , Proteínas de Drosophila/metabolismo , Drosophila melanogaster/citologia , Drosophila melanogaster/metabolismo , Proteínas de Membrana/metabolismo , Morfogênese , Animais , Proteínas de Drosophila/genética , Drosophila melanogaster/embriologia , Drosophila melanogaster/genética , Proteínas de Membrana/genética , Traqueia/citologia , Traqueia/embriologia , Traqueia/metabolismo
10.
Development ; 134(7): 1337-46, 2007 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-17329358

RESUMO

In Drosophila, restricted expression of the Iroquois complex (Iro-C) genes in the proximal region of the wing imaginal disc contributes to its territorial subdivision, specifying first the development of the notum versus the wing hinge, and subsequently, that of the lateral versus medial notum. Iro-C expression is under the control of the EGFR and Dpp signalling pathways. To analyze how both pathways cooperate in the regulation of Iro-C, we isolated several wing disc-specific cis-regulatory elements of the complex. One of these (IroRE(2)) integrates competing inputs of the EGFR and Dpp pathways, mediated by the transcription factors Pointed (downstream of EGFR pathway) and Pannier/U-shaped and Mothers against Dpp (Mad), in the case of Dpp. By contrast, a second element (IroRE(1)) mediates activation by both the EGFR and Dpp pathways, thus promoting expression of Iro-C in a region of elevated levels of Dpp signalling, the prospective lateral notum near the anterior-posterior compartment boundary. These results help define the molecular mechanisms of the interplay between the EGFR and Dpp pathways in the specification and patterning of the notum.


Assuntos
Padronização Corporal/fisiologia , Proteínas de Drosophila/metabolismo , Drosophila/embriologia , Receptores ErbB/metabolismo , Regulação da Expressão Gênica no Desenvolvimento , Proteínas de Homeodomínio/metabolismo , Proteínas Quinases/metabolismo , Receptores de Peptídeos de Invertebrados/metabolismo , Transdução de Sinais/fisiologia , Tórax/embriologia , Animais , Primers do DNA , Proteínas de Ligação a DNA/metabolismo , Drosophila/metabolismo , Imuno-Histoquímica , Mutagênese , Proteínas do Tecido Nervoso/metabolismo , Proteínas Proto-Oncogênicas/metabolismo , Análise de Sequência de DNA , Fatores de Transcrição/metabolismo
11.
Mol Cell ; 23(5): 631-40, 2006 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-16949360

RESUMO

The PB1-domain-containing proteins p62, aPKC, MEKK2/MEKK3, MEK5, and Par-6 play roles in critical cell processes like osteoclastogenesis, angiogenesis, and early cardiovascular development or cell polarity. PB1 domains are scaffold modules that adopt the topology of ubiquitin-like beta-grasp folds that interact with each other in a front-to-back mode to arrange heterodimers or homo-oligomers. The different PB1 domain adaptors provide specificity for PB1 kinases to ensure the effective transmission of cellular signals. Also, recent data suggest that PB1 domains may serve to orchestrate signaling cascades not involving other PB1 domains, such as the MEK5-ERK5 and p62-ERK1 interactions.


Assuntos
Proteínas Nucleares/química , Proteínas Nucleares/metabolismo , Transdução de Sinais , Fatores de Transcrição/química , Fatores de Transcrição/metabolismo , Proteínas Adaptadoras de Transdução de Sinal , Animais , Proteínas de Ligação a DNA , Humanos , Inflamação , Ligação Proteica , Estrutura Terciária de Proteína , Proteínas/metabolismo , Proteína Sequestossoma-1
12.
Genetica ; 122(3): 311-24, 2004 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-15609554

RESUMO

The 3A and 60E regions of Drosophila melanogaster polytene chromosomes containing inserted copies of the P[1ArB] transposon have been subjected to an electron microscopic (EM) analysis. We show that both inserts led to formation of new bands within the interband regions 3A4/A6 and 60E8-9/E10. This allowed us to clone DNA of these interbands. Their sequences, as well as those of DNA from other four interbands described earlier, have been analyzed. We have found that, with the exception of 60E8-9/E10 interband, all other five regions under study corresponded to 5' or 3' ends of genes. We have further obtained the evidence for 60E8-9/E10 interband to harbor the 'housekeeping' RpL19 gene, which is transcribed in many tissues, including salivary glands. Based upon the genetic heterogeneity of the interbands observed a revised model of polytene chromosome organization is discussed.


Assuntos
Cromossomos/genética , Drosophila melanogaster/genética , Animais , Bandeamento Cromossômico , Cromossomos/fisiologia , Cromossomos/ultraestrutura , Clonagem Molecular , Elementos de DNA Transponíveis , Microscopia Eletrônica , Análise de Sequência de DNA
13.
J Cell Biol ; 166(4): 549-57, 2004 Aug 16.
Artigo em Inglês | MEDLINE | ID: mdl-15302858

RESUMO

Both in Drosophila and vertebrate epithelial cells, the establishment of apicobasal polarity requires the apically localized, membrane-associated Par-3-Par-6-aPKC protein complex. In Drosophila, this complex colocalizes with the Crumbs-Stardust (Sdt)-Pals1-associated TJ protein (Patj) complex. Genetic and molecular analyses suggest a functional relationship between them. We show, by overexpression of a kinase-dead Drosophila atypical PKC (DaPKC), the requirement for the kinase activity of DaPKC to maintain the position of apical determinants and to restrict the localization of basolateral ones. We demonstrate a novel physical interaction between the apical complexes, via direct binding of DaPKC to both Crb and Patj, and identify Crumbs as a phosphorylation target of DaPKC. This phosphorylation of Crumbs is functionally significant. Thus, a nonphosphorylatable Crumbs protein behaves in vivo as a dominant negative. Moreover, the phenotypic effect of overexpressing wild-type Crumbs is suppressed by reducing DaPKC activity. These results provide a mechanistic framework for the functional interaction between the Par-3-Par-6-aPKC and Crumbs-Sdt-Patj complexes based in the posttranslational modification of Crb by DaPKC.


Assuntos
Proteínas de Drosophila/metabolismo , Células Epiteliais/citologia , Proteínas de Membrana/metabolismo , Proteína Quinase C/metabolismo , Sequência de Aminoácidos , Animais , Padronização Corporal , Polaridade Celular , DNA Complementar/metabolismo , Drosophila , Regulação da Expressão Gênica no Desenvolvimento , Biblioteca Gênica , Genes Dominantes , Glutationa Transferase/metabolismo , Imuno-Histoquímica , Dados de Sequência Molecular , Mutagênese Sítio-Dirigida , Mutação , Fosforilação , Ligação Proteica , Processamento de Proteína Pós-Traducional , Proteínas Recombinantes de Fusão/metabolismo , Junções Íntimas , Asas de Animais/metabolismo
15.
Eur J Biochem ; 270(2): 293-306, 2003 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-12605680

RESUMO

Four distinct eukaryotic initiation factor 2alpha (eIF2alpha) kinases phosphorylate eIF2alpha at S51 and regulate protein synthesis in response to various environmental stresses. These are the hemin-regulated inhibitor (HRI), the interferon-inducible dsRNA-dependent kinase (PKR), the endoplasmic reticulum (ER)-resident kinase (PERK) and the GCN2 protein kinase. Whereas HRI and PKR appear to be restricted to mammalian cells, GCN2 and PERK seem to be widely distributed in eukaryotes. In this study, we have characterized the second eIF2alpha kinase found in Drosophila, a PERK homologue (DPERK). Expression of DPERK is developmentally regulated. During embryogenesis, DPERK expression becomes concentrated in the endodermal cells of the gut and in the germ line precursor cells. Recombinant wild-type DPERK, but not the inactive DPERK-K671R mutant, exhibited an autokinase activity, specifically phosphorylated Drosophila eIF2alpha at S50, and functionally replaced the endogenous Saccharomyces cerevisiae GCN2. The full length protein, when expressed in 293T cells, located in the ER-enriched fraction, and its subcellular localization changed with deletion of different N-terminal fragments. Kinase activity assays with these DPERK deletion mutants suggested that DPERK localization facilitates its in vivo function. Similar to mammalian PERK, DPERK forms oligomers in vivo and DPERK activity appears to be regulated by ER stress. Furthermore, the stable complexes between wild-type DPERK and DPERK-K671R mutant were mediated through the N terminus of the proteins and exhibited an in vitro eIF2alpha kinase activity.


Assuntos
Drosophila melanogaster/metabolismo , Fator de Iniciação 2 em Eucariotos/metabolismo , eIF-2 Quinase/metabolismo , Sequência de Aminoácidos , Animais , Drosophila melanogaster/embriologia , Drosophila melanogaster/genética , Retículo Endoplasmático/metabolismo , Perfilação da Expressão Gênica , Dados de Sequência Molecular , Fosforilação , Proteínas Quinases/metabolismo , Proteínas Serina-Treonina Quinases , Estrutura Terciária de Proteína , Saccharomyces cerevisiae , Proteínas de Saccharomyces cerevisiae , Análise de Sequência de DNA , Análise de Sequência de Proteína , eIF-2 Quinase/genética
16.
EMBO J ; 21(13): 3327-36, 2002 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-12093734

RESUMO

Grim encodes a protein required for programmed cell death in Drosophila. The Grim N-terminus induces apoptosis by disrupting IAP blockage of caspases; however, N-terminally-deleted Grim retains pro apoptotic activity. We describe GH3, a 15 amino acid internal Grim domain absolutely required for its proapoptotic activity and sufficient to induce cell death when fused to heterologous carrier proteins. A GH3 homology region is present in the Drosophila proapoptotic proteins Reaper and Sickle. The GH3 domain and the homologous regions in Reaper and Sickle are predicted to be structured as amphipathic alpha-helixes. During apoptosis induction, Grim colocalizes with mitochondria and cytochrome c in a GH3-dependent but N-terminal- and caspase activity-independent manner. When Grim is overexpressed in vivo, both the N-terminal and the GH3 domains are equally necessary, and cooperate for apoptosis induction. The N-terminal and GH3 Grim domains thus activate independent apoptotic pathways that synergize to induce programmed cell death efficiently.


Assuntos
Apoptose/fisiologia , Proteínas de Drosophila/fisiologia , Drosophila melanogaster/citologia , Mitocôndrias/fisiologia , Neuropeptídeos/fisiologia , Sequência de Aminoácidos , Substituição de Aminoácidos , Animais , Animais Geneticamente Modificados , Caspases/fisiologia , Células Cultivadas , Grupo dos Citocromos c/fisiologia , Proteínas de Drosophila/química , Feminino , Masculino , Dados de Sequência Molecular , Neuropeptídeos/química , Fenótipo , Estrutura Terciária de Proteína , Proteínas Recombinantes de Fusão/fisiologia , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos , Relação Estrutura-Atividade
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