Relevant bibliographies by topics / G proteins ; Drosophila

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Academic literature on the topic 'G proteins ; Drosophila'

Author: Grafiati
Published: 4 June 2021
Last updated: 8 February 2022

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Journal articles on the topic "G proteins ; Drosophila"

1

Wadsworth, Samuel C. "Drosophila src family proteins." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 97, no. 3 (January 1990): 403–6. http://dx.doi.org/10.1016/0305-0491(90)90135-g.

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Schmidt, C. J., S. Garen-Fazio, Y. K. Chow, and E. J. Neer. "Neuronal expression of a newly identified Drosophila melanogaster G protein alpha 0 subunit." Cell Regulation 1, no. 1 (November 1989): 125–34. http://dx.doi.org/10.1091/mbc.1.1.125.

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Guanine nucleotide-binding proteins (G proteins) mediate signals between activated cell-surface receptors and cellular effectors. A bovine G-protein alpha-subunit cDNA has been used to isolate similar sequences from Drosophila genomic and cDNA libraries. One class, which we call DG alpha 0, hybridized to position 47A on the second chromosome of Drosophila. The nucleotide sequence of the protein coding region of one cDNA has been determined, revealing an alpha subunit that is 81% identical with rat alpha 0. The cDNA hybridizes strongly to a 3.8 kb mRNA and weakly with a 5.3 kb message. Antibodies raised against a trp-E-DG alpha 0 fusion protein recognized a 39,000 Da protein in Drosophila extracts. In situ hybridization to adult Drosophila sections combined with immunohistochemical studies revealed expression throughout the optic lobes and central brain and in the thoracic and abdominal ganglia. DG alpha 0 message and protein were also detected in the antennae, oocytes, and ovarian nurse cells. The neuronal expression of this gene is similar to mammalian alpha 0, which is most abundantly expressed in the brain.
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van Lohuizen, Maarten, Marieke Tijms, Jan Willem Voncken, Armin Schumacher, Terry Magnuson, and Ellen Wientjens. "Interaction of Mouse Polycomb-Group (Pc-G) Proteins Enx1 and Enx2 with Eed: Indication for Separate Pc-G Complexes." Molecular and Cellular Biology 18, no. 6 (June 1, 1998): 3572–79. http://dx.doi.org/10.1128/mcb.18.6.3572.

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ABSTRACT The Polycomb group (Pc-G) constitutes an important, functionally conserved group of proteins, required to stably maintain inactive homeobox genes repressed during development. Drosophila extra sex combs (esc) and its mammalian homolog embryonic ectoderm development (eed) are special Pc-G members, in that they are required early during development when Pc-G repression is initiated, a process that is still poorly understood. To get insight in the molecular function of Eed, we searched for Eed-interacting proteins, using the yeast two-hybrid method. Here we describe the specific in vivo binding of Eed to Enx1 and Enx2, two mammalian homologs of the essential DrosophilaPc-G gene Enhancer-of-zeste[E(z)]. No direct biochemical interactions were found between Eed/Enx and a previously characterized mouse Pc-G protein complex, containing several mouse Pc-G proteins includingmouse polyhomeotic (Mph1). This suggests that different Pc-G complexes with distinct functions may exist. However, partial colocalization of Enx1 and Mph1 to subnuclear domains may point to more transient interactions between these complexes, in support of a bridging role for Enx1.
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Katanayeva, Natalya, Damir Kopein, Reto Portmann, Daniel Hess, and Vladimir L. Katanaev. "Competing Activities of Heterotrimeric G Proteins in Drosophila Wing Maturation." PLoS ONE 5, no. 8 (August 23, 2010): e12331. http://dx.doi.org/10.1371/journal.pone.0012331.

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Wolfgang, W. J., F. Quan, N. Thambi, and M. Forte. "Restricted spatial and temporal expression of G-protein alpha subunits during Drosophila embryogenesis." Development 113, no. 2 (October 1, 1991): 527–38. http://dx.doi.org/10.1242/dev.113.2.527.

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Of the known signal transduction mechanisms, the most evolutionarily ancient is mediated by a family of heterotrimeric guanine nucleotide binding proteins or G proteins. In simple organisms, this form of sensory transduction is used exclusively to convey signals of developmental consequence. In metazoan organisms, however, the developmental role of G-protein-coupled sensory transduction has been more difficult to elucidate because of the wide variety of signals (peptides, small molecules, odorants, hormones, etc.) that use this form of sensory transduction. We have begun to examine the role of G-protein-coupled signaling during development by investigating the expression during Drosophila embryogenesis of a limited set of G proteins. Since these proteins are a common component of all G-protein-coupled signaling systems, their developmental pattern of expression should indicate when and where programmed changes in gene activity are initiated by, or involve the participation of, G-protein-coupled signaling events. We have focused on the spatial and temporal expression pattern of three different Drosophila G-protein alpha subunits by northern blot analysis, in situ hybridization and immunocytochemistry using antibodies directed to peptides specifically found in each alpha subunit. From the spatial and temporal restriction of the expression of each protein, our results suggest that different forms of G-protein-coupled sensory transduction may mediate developmental interactions during both early and late stages of embryogenesis and may participate in a variety of specific developmental processes such as the establishment of embryonic position, the ontogeny of the nervous system and organogenesis.
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Chamberlin, H. M., and J. H. Thomas. "The bromodomain protein LIN-49 and trithorax-related protein LIN-59 affect development and gene expression in Caenorhabditis elegans." Development 127, no. 4 (February 15, 2000): 713–23. http://dx.doi.org/10.1242/dev.127.4.713.

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We have molecularly characterized the lin-49 and lin-59 genes in C. elegans, and found their products are related to Drosophila trithorax group (trx-G) proteins and other proteins implicated in chromatin remodelling. LIN-49 is structurally most similar to the human bromodomain protein BR140, and LIN-59 is most similar to the Drosophila trx-G protein ASH1. In C. elegans, lin-49 and lin-59 are required for the normal development of the mating structures of the adult male tail, for the normal morphology and function of hindgut (rectum) cells in both males and hermaphrodites and for the maintenance of structural integrity in the hindgut and egg-laying system in adults. Expression of the Hox genes egl-5 and mab-5 is reduced in lin-49 and lin-59 mutants, suggesting lin-49 and lin-59 regulate HOM-C gene expression in C. elegans as the trx-G genes do in Drosophila. lin-49 and lin-59 transgenes are expressed widely throughout C. elegans animals. Thus, in contrast to the C. elegans Polycomb group (Pc-G)-related genes mes-2 and mes-6 that function primarily in the germline, we propose lin-49 and lin-59 function in somatic development similar to the Drosophila trx-G genes.
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Kopein, Damir, and Vladimir L. Katanaev. "Drosophila GoLoco-Protein Pins Is a Target of Gαo-mediated G Protein–coupled Receptor Signaling." Molecular Biology of the Cell 20, no. 17 (September 2009): 3865–77. http://dx.doi.org/10.1091/mbc.e09-01-0021.

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G protein–coupled receptors (GPCRs) transduce their signals through trimeric G proteins, inducing guanine nucleotide exchange on their Gα-subunits; the resulting Gα-GTP transmits the signal further inside the cell. GoLoco domains present in many proteins play important roles in multiple trimeric G protein–dependent activities, physically binding Gα-subunits of the Gαi/o class. In most cases GoLoco binds exclusively to the GDP-loaded form of the Gα-subunits. Here we demonstrate that the poly-GoLoco–containing protein Pins of Drosophila can bind to both GDP- and GTP-forms of Drosophila Gαo. We identify Pins GoLoco domain 1 as necessary and sufficient for this unusual interaction with Gαo-GTP. We further pinpoint a lysine residue located centrally in this domain as necessary for the interaction. Our studies thus identify Drosophila Pins as a target of Gαo-mediated GPCR receptor signaling, e.g., in the context of the nervous system development, where Gαo acts downstream from Frizzled and redundantly with Gαi to control the asymmetry of cell divisions.
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Yamamoto, Y., F. Girard, B. Bello, M. Affolter, and W. J. Gehring. "The cramped gene of Drosophila is a member of the Polycomb-group, and interacts with mus209, the gene encoding Proliferating Cell Nuclear Antigen." Development 124, no. 17 (September 1, 1997): 3385–94. http://dx.doi.org/10.1242/dev.124.17.3385.

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We have isolated and molecularly characterized the cramped (crm) gene of Drosophila melanogaster, and show that it can be classified as a Polycomb-group (Pc-G) gene. crm mutants exhibit typical Pc-G mutant phenotypes, reminiscent of ectopic homeotic gene expression, with additional sex comb teeth found on mesothoracic and metathoracic legs, and proximodistal transformations of the tarsal segments. crm encodes an 693 amino acids protein, with no significant homology to known proteins. We used polyclonal antibodies raised against bacterially expressed truncated CRM protein to show that the crm gene product is localized to the nucleus during embryogenesis. This nuclear localization appears to be restricted to S-phase nuclei, as CRM immunostaining disappears at mitosis. We found that this cell-cycle-dependent staining pattern was identical to that of Proliferating Cell Nuclear Antigen (PCNA). Furthermore, we provide evidence for co-localization of CRM and PCNA proteins in salivary gland polytene nuclei, and for a genetic interaction between crm and mus209, the Drosophila gene encoding PCNA. Together, our data suggest that these two proteins are involved in a common regulatory pathway and highlight possible interactions between Pc-G-mediated silencing and DNA replication in Drosophila.
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Bunker, C. A., and R. E. Kingston. "Transcriptional repression by Drosophila and mammalian Polycomb group proteins in transfected mammalian cells." Molecular and Cellular Biology 14, no. 3 (March 1994): 1721–32. http://dx.doi.org/10.1128/mcb.14.3.1721.

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The Polycomb group (Pc-G) genes are essential for maintaining the proper spatially restricted expression pattern of the homeotic loci during Drosophila development. The Pc-G proteins appear to function at target loci to maintain a state of transcriptional repression. The murine oncogene bmi-1 has significant homology to the Pc-G gene Posterior sex combs (Psc) and a highly related gene, Suppressor two of zeste [Su(z)2]. We show here that the proteins encoded by bmi-1 and the Pc-G genes Polycomb (Pc) and Psc as well as Su(z)2 mediate repression in mammalian cells when targeted to a promoter by LexA in a cotransfection system. These fusion proteins repress activator function by as much as 30-fold, and the effect on different activation domains is distinct for each Pc-G protein. Repression is observed when the LexA fusion proteins are bound directly adjacent to activator binding sites and also when bound 1,700 bases from the promoter. These data demonstrate that the products of the Pc-G genes can significantly repress activator function on transiently introduced DNA. We suggest that this function contributes to the stable repression of targeted loci during development.
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Bunker, C. A., and R. E. Kingston. "Transcriptional repression by Drosophila and mammalian Polycomb group proteins in transfected mammalian cells." Molecular and Cellular Biology 14, no. 3 (March 1994): 1721–32. http://dx.doi.org/10.1128/mcb.14.3.1721-1732.1994.

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The Polycomb group (Pc-G) genes are essential for maintaining the proper spatially restricted expression pattern of the homeotic loci during Drosophila development. The Pc-G proteins appear to function at target loci to maintain a state of transcriptional repression. The murine oncogene bmi-1 has significant homology to the Pc-G gene Posterior sex combs (Psc) and a highly related gene, Suppressor two of zeste [Su(z)2]. We show here that the proteins encoded by bmi-1 and the Pc-G genes Polycomb (Pc) and Psc as well as Su(z)2 mediate repression in mammalian cells when targeted to a promoter by LexA in a cotransfection system. These fusion proteins repress activator function by as much as 30-fold, and the effect on different activation domains is distinct for each Pc-G protein. Repression is observed when the LexA fusion proteins are bound directly adjacent to activator binding sites and also when bound 1,700 bases from the promoter. These data demonstrate that the products of the Pc-G genes can significantly repress activator function on transiently introduced DNA. We suggest that this function contributes to the stable repression of targeted loci during development.
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Dissertations / Theses on the topic "G proteins ; Drosophila"

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Srivastava, Deepak Prakash. "Characterisation of a novel Drosophila G-protein coupled receptor differentially activated by catecholamines and steroids." Thesis, University of Cambridge, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.614677.

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Ignatious, Raja Jennifer Sinthiya [Verfasser]. "Role of G proteins in olfactory signaling of Drosophila / Jennifer Sinthiya Ignatious Raja." Konstanz : Bibliothek der Universität Konstanz, 2013. http://d-nb.info/1078229627/34.

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Birkholz, Denise A. "Photoreceptor cell fate determination and rhodopsin expression in the developing eye of Drosophila /." Connect to full text via ProQuest. IP filtered, 2005.

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Nipper, Rick William Jr 1978. "Molecular function of the cell polarity protein partner of inscuteable in Drosophila neuroblasts." Thesis, University of Oregon, 2007. http://hdl.handle.net/1794/6194.

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xiii, 48 p. : (col. ill.) A print copy of this title is available through the UO Libraries under the call number: SCIENCE QL537.D76 N57 2007
Asymmetric cell division (ACD) is a unique mechanism employed during development to achieve cellular diversity from a small number of progenitor cells. Cells undergoing ACD distribute factors for self-renewal at the apical cortex and factors for differentiation at the basal cortex. It is critical for proper development that the mitotic spindle be tightly coupled to this axis of polarization such that both sets of proteins are exclusively segregated into the daughter cells. We use ACD in Drosophila neuroblasts as a model system for understanding the molecular mechanisms that govern spindle-cortical coupling. Neuroblasts polarize Partner of Inscuteable (Pins), Gαi and Mushroom Body Defect (Mud) at the apical cell cortex during mitosis. Gαi and Pins are required for establishing cortical polarity while Mud is essential for spindle-cortical alignment. Gαi and Mud interact through Pins GoLoco domains and tetratricopeptide repeats (TPR) respectively, however it is unclear how Mud activity is integrated with Pins and Gαi to link neuroblast cortical polarity to the mitotic spindle. This dissertation describes how Pins interactions with Gαi and Mud regulate Iwo fundamental aspects of neuroblast ACD: cortical polarity and alignment of the spindle with the resulting polarity axis. I demonstrate that Pins is a dynamic scaffolding protein that undergoes a GoLoco-TPR intramolecular interaction, resulting in a conformation of Pins with low Mud and reduced Gαi binding affinity. However, Pins TPR domains fail to completely repress Gαi binding, as a single GoLoco is unaffected by the intramolecular isomerization. Gαi present at the apical cortex specifies Pins localization through binding this "unregulated" GoLoco. Liberation of Pins intramolecularly coupled state occurs through cooperative binding of Gαi and Mud to the other GoLoco and TPR domains, creating a high-affinity Gαi-Pins-Mud complex. This autoregulatory mechanism spatially confines the Pins-Mud interaction to the apical cortex and facilitates proper apical-spindle orientation. In conclusion, these results suggest Gαi induces multiple Pins states to both properly localize Pins and ensure tight coupling between apical polarity and mitotic spindle alignment.
Adviser: Ken Prehoda
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Ni, Lina. "Maintenance of Visual Sensitivity in the Drosophila Eye: A Dissertation." eScholarship@UMMS, 2010. https://escholarship.umassmed.edu/gsbs_diss/457.

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High visual sensitivity is a common but important characteristic of animal eyes. It is especially critical for night vision. In animal eyes, photoreceptors are the first to receive the incoming rays of light and they convert the light signals to electrical signals before passing the information to interneurons in the eye and finally to the brain. To function in dim light conditions, photoreceptors have developed high sensitivities to light. It is reported that both mammalian rod photoreceptors and Drosophilaphotoreceptors can detect single photons. The high sensitivities of photoreceptors largely depend on a high content of rhodopsin, a light-stimulated G protein-coupled receptor (GPCR), in light sensory organelles, outer segments in mammals and rhabdomeres in Drosophila. Two shared characteristics, the tightly packed photoreceptive membrane and the high concentration of rhodopsin in the membrane, work together to enable the photoreceptors to achieve the high content of rhodopsin in photosensory organelles in both mammals and Drosophila. In this thesis, I have used the Drosophilaeye as a model system to study the molecular mechanisms required for the maintenance of these two characteristics. In the second chapter, I present a new molecular mechanism of preventing Gq-mediated rhabdomeral degeneration. A new gene named tadr (for torn and diminished rhabdomeres), when mutated, leads to visual sensitivity reduction and photoreceptor degeneration. Degeneration in the tadr mutant is characterized by shrunken and disrupted rhabdomeres. The TADR protein interacts in vitro with the major light receptor Rh1 rhodopsin, and genetic reduction of the Rh1 level suppresses the tadr-induced degeneration, suggesting the degeneration is Rh1-dependent. Nonetheless, removal of phospholipase C (PLC), a key enzyme in phototransduction, and that of Arr2 fail to inhibit rhabdomeral degeneration in the tadr mutant background. Biochemical analyses reveal that, in the tadr mutant, the Gq protein of Rh1 is defective in dissociation from the membrane during light stimulation. Importantly, reduction of Gq level by introducing a hypomorphic allele of Gαq gene greatly inhibits the tadr degeneration phenotype. These results may suggest that loss of a potential TADR-Rh1 interaction leads to an abnormality in the Gqsignaling, which in turn triggers rhabdomeral degeneration independent of the PLC phototransduction cascade. We propose that TADR-like proteins may also protect photoreceptors from degeneration in mammals including humans. In the third chapter, I present a Drosophila CUB- and LDLa-domain transmembrane protein CULD that counteracts the visual arrestin Arr1-mediated endocytosis to retain rhodopsin in rhabdomeral membrane. CULD is mostly localized in rhabdomeres, but is also detected in scarce rhodopsin endocytic vesicles that contain Arr1. An intracellular region of CULD interacts with Arr1 in vitro. In both culdmutant and knockdown flies, a large amount of rhodopsin is mislocalized in the cell body of photoreceptors through lightdependent, Arr1-mediated endocytosis, leading to reduction of photoreceptor sensitivity. Expressing a wild-type CULD protein in photoreceptors, but not a mutant variant lacking the Arr1-interacting site, rescues both the rhodopsin mislocalization and the low sensitivity phenotypes. Once rhodopsin has been internalized in adult mutant flies, it is reversed only by expression of CULD but not by blocking endocytosis, suggesting that CULD promotes recycling of endocytosed rhodopsin to the rhabdomere. Our results demonstrate an important role of CULD in the maintenance of membrane rhodopsin density and photoreceptor sensitivity. We propose that a common cellular function of CUB- and LDLa-domain proteins, in both mammals and invertebrates, is to concentrate receptors including GPCRs in particular regions of cell membrane. In summary, the work addressed in this thesis has identified new molecular mechavii nisms underlying the maintenance of visual sensitivity in Drosophila, either through preventing Gq-mediated rhabdomeral degeneration or through antagonizing arrestin-mediated rhodopsin endocytosis. This work has advanced our understanding of visual biology and the general regulatory mechanisms of GPCR signaling, and may provide valuable clues to pathologic studies of human retinal degeneration disorders.
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Forsthoefel, David J. "A molecular genetic analysis of the role of the Guanine Nucleotide Exchange Factor Trio during Axon Pathfinding in the Embryonic CNS of Drosophila melanogaster." Connect to resource, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1127241654.

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Pathirana, Stephen. "G-protein signalling is essential for Drosophila oogenesis." Thesis, University of Edinburgh, 2000. http://hdl.handle.net/1842/11237.

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Starting from a gal4/UAS enhancer trap screen, Dr Zhao isolated two cDNAs encoded by a gene expressed in anterior dorsal follicle cells. I sequenced these and identified them as members of a new family of RGS proteins responsible for the negative regulation of G-Protein signalling. This gene was also identified by Granderath et al.
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Schuette, Diana Gisela. "Characterisation of G-protein-coupled serotonin receptors in insect cells." Thesis, Oxford Brookes University, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.363747.

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Duncanson, Audrey. "Genetic analysis of G protein-coupled signalling pathways in Drosophila melanogaster." Thesis, University of Glasgow, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337512.

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Umukoro, Oghenetega Francisca. "The effects of alcohol on G protein gene expression in Drosophila melanogaster." Thesis, University of East London, 2015. http://roar.uel.ac.uk/4558/.

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Alcohol is one of the most widely used and socially acceptable drugs in the world. However, its chronic use can lead to serious problems including the development of tolerance. Acute and chronic use of ethanol leads to short-term and long-term changes in gene expression in the brain resulting in cellular and molecular adaptations that are associated with addictive behaviours. Our understanding of the mechanisms by which alcohol produces these changes in the brain is not fully understood. Ethanol affects the function of receptors including G protein-coupled receptors that activate heterotrimeric G proteins. The aim of this thesis is to understand whether ethanol can cause changes in G protein gene expression using Drosophila melanogaster as a model. Drosophila is a genetically tractable organism suitable to investigate the neural substrates of neuroadaptive responses to ethanol. The response to ethanol and the onset of tolerance was measured in wild-type and mutant Drosophila. While tolerance was consistently observed in all fly populations, individual differences in sensitivity to alcohol were observed, which prompted the isolation of subpopulations of Drosophila with distinct ethanol characteristics. Relative mRNA expression in G protein subunits was measured using quantitative real-time polymerase chain reaction in different Drosophila strains (wild-type, subpopulations of early and late responders, G protein mutants and dopamine 1-like D2 receptor mutants) that have received zero, one, two or three ethanol exposures at 24 h intervals. When measured in the wild-type strains, changes in G protein subunits expression were variable. However in a subpopulations of early responders that were selected for high ethanol sensitivity, a non-statistically significant decrease of two Gα-protein subunits: Gi and Gq were observed. When measured in two Drosophila mutant strains, flies with ii either deletion of dopamine D2 receptor or a mutated Gi gene subunit, statistically significant changes were observed in Gi and Gq subunits. In a further study, a mutant expressing non-functional Gq, the Gi expression was not affected by the ethanol treatment suggesting a possible crosstalk between different signalling pathways. These results justify a more detailed investigation of changes in G protein subunits following acute and chronic exposure to ethanol in Drosophila, which will allow verifying the hypothesis that changes in gene expression of G proteins participate in addictive behaviours in Drosophila. These findings in Drosophila, which share genetic and functional characteristics with the mammalian nervous system, could translate into important advances in identifying targets for treatment for alcohol addiction in humans.
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Book chapters on the topic "G proteins ; Drosophila"

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Brillet, Karl, Carlos A. Pereira, and Renaud Wagner. "Expression of Membrane Proteins in Drosophila Melanogaster S2 Cells: Production and Analysis of a EGFP-Fused G Protein-Coupled Receptor as a Model." In Methods in Molecular Biology, 119–33. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-344-2_8.

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HURLEY, JAMES B. "G Proteins of Drosophila melanogaster." In Signal Transduction, 377–89. Elsevier, 1993. http://dx.doi.org/10.1016/b978-0-12-429350-2.50019-x.

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Yu, Fengwei. "Analysis of the Roles of Pins and Heterotrimeric G Proteins in Asymmetric Division of Drosophila Neuroblasts." In Regulators of G-Protein Signaling, Part A, 364–82. Elsevier, 2004. http://dx.doi.org/10.1016/s0076-6879(04)89022-0.

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Granderath, Sebastian, and Christian Klämbt. "Identification and Functional Analysis of the Drosophila Gene loco." In Regulators of G-Protein Signaling, Part A, 350–63. Elsevier, 2004. http://dx.doi.org/10.1016/s0076-6879(04)89021-9.

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