LncRNA ‐ IRAR ‐mediated regulation of insulin receptor transcripts in Drosophila melanogaster during nutritional stress

2021 ◽  
Author(s):  
Jie Chen ◽  
Yuantai Huang ◽  
Guojun Qi
Keyword(s):  
Drosophila Melanogaster ◽  
Insulin Receptor ◽  
Nutritional Stress

scholarly journals Tissue localization of Drosophila melanogaster insulin receptor transcripts during development.

1988 ◽  
Vol 8 (4) ◽  
pp. 1638-1647 ◽  
Author(s):  
R S Garofalo ◽  
O M Rosen
Keyword(s):  
Nervous System ◽  
Drosophila Melanogaster ◽  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Protein Tyrosine Kinase ◽  
Kinase Activity ◽  
Ganglion Cells ◽  
Northern Analysis ◽  
Tyrosine Kinase Domain ◽  
Subunit Structure

The Drosophila melanogaster insulin receptor (Drosophila insulin receptor homolog [dIRH]) is similar to its mammalian counterpart in deduced amino acid sequence, subunit structure, and ligand-stimulated protein tyrosine kinase activity. The function of this receptor in D. melanogaster is not yet known. However, a role in development is suggested by the observations that levels of insulin-stimulated kinase activity and expression of dIRH mRNA are maximal during Drosophila midembryogenesis. In this study, a 2.9-kilobase (kb) cDNA clone corresponding to both the dIRH tyrosine kinase domain and some of the 3' untranslated sequence was used to determine the tissue distribution of dIRH mRNA during development. Two principal mRNAs of 11 and 8.6 kb hybridized with the dIRH cDNA in Northern (RNA) blot analysis. The abundance of the 8.6-kb mRNA increased transiently in early embryos, whereas the 11-kb species was most abundant during midembryogenesis. A similar pattern of expression was previously determined by Northern analysis, using a dIRH genomic clone (L. Petruzzelli, R. Herrera, R. Arenas-Garcia, R. Fernandez, M. J. Birnbaum, and O. M. Rosen, Proc. Natl. Acad. Sci. USA 83:4710-4714, 1986). In situ hybridization revealed dIRH transcripts in the ovaries of adult flies, in which the transcripts appeared to be synthesized by nurse cells for eventual storage as maternal RNA in the mature oocyte. Throughout embryogenesis, dIRH transcripts were ubiquitously expressed, although after midembryogenesis, higher levels were detected in the developing nervous system. Nervous system expression remained elevated throughout the larval stages and persisted in the adult, in which the cortex of the brain and ganglion cells were among the most prominently labeled tissues. In larvae, the imaginal disk cells exhibited comparatively high levels of dIRH mRNA expression. The broad distribution of dIRH mRNA in embryos and imaginal disks is compatible with a role for dIRH in anabolic processes required for cell growth. The apparently elevated expression of dIRH mRNA in nervous tissue during mid- and late embryogenesis coincides with a period of active neurite outgrowth and suggests that dIRH may be involved in this process.

scholarly journals Modularity and hormone sensitivity of the Drosophila melanogaster insulin receptor/target of rapamycin interaction proteome

2011 ◽  
Vol 7 (1) ◽  
pp. 547 ◽  
Author(s):  
Timo Glatter ◽  
Ralf B Schittenhelm ◽  
Oliver Rinner ◽  
Katarzyna Roguska ◽  
Alexander Wepf ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Insulin Receptor ◽  
Target Of Rapamycin ◽  
Hormone Sensitivity

scholarly journals Impact of Probiotic Combination in InR[E19]/TM2 Drosophila melanogaster on Longevity, Related Gene Expression, and Intestinal Microbiota: A Preliminary Study

2020 ◽  
Vol 8 (7) ◽  
pp. 1027
Author(s):  
Shuang Ma ◽  
Hao Sun ◽  
Weichao Yang ◽  
Mingfu Gao ◽  
Hui Xu
Keyword(s):  
Drosophila Melanogaster ◽  
Insulin Receptor ◽  
Insulin Signaling ◽  
High Throughput Sequencing ◽  
Metabolic Diseases ◽  
Standard Diet ◽  
Median Lifespan ◽  
Treatment Of Diabetes ◽  
Receptor Family

The insulin receptor (InR) pertains to the insulin receptor family, which plays a key role in the insulin/insulin-like growth factor (IGF)-like signaling (IIS) pathway. Insulin signaling defects may result in the development of metabolic diseases, such as type 2 diabetes, and the InR mutant has been suggested to bear insulin signaling deficiency. Numerous studies have reported that probiotics are beneficial for the treatment of diabetes; however, the effect of probiotics on patients with InR deficiency has seldom been reported. Therefore, we chose the InR[E19]/TM2 Drosophila melanogaster to investigate. The results indicated that probiotics significantly reduce the mean and median lifespan of InR[E19]/TM2 Drosophila (by 15.56% and 23.82%, respectively), but promote that of wild-type files (by 9.31% and 16.67%, respectively). Significant differences were obtained in the expression of lifespan- and metabolism-related genes, such as Imp-L2, Tor, and GstD2, between the standard diet groups and the probiotics groups. Furthermore, analysis of 16S rDNA via high throughput sequencing revealed that the gut bacterial diversity of Drosophila fed with a probiotic combination also differs from that of Drosophila fed with a standard diet. In summary, these findings indicate that a probiotic combination indeed affects InR[E19]/TM2 Drosophila, but not all of its impacts are positive.

Comparative modeling of the phosphatase and kinase domains of protein tyrosine phosphatase and insulin receptor kinase from Drosophila melanogaster (DPTP61fm), and a computational study of their mutual interactions

2002 ◽  
Vol 80 (2) ◽  
pp. 225-239 ◽  
Author(s):  
Sanchita Hati ◽  
Sudeep Bhattacharyya ◽  
James V Price ◽  
Alan S Tracey
Keyword(s):  
Hydrogen Bonding ◽  
Drosophila Melanogaster ◽  
Insulin Receptor ◽  
Protein Tyrosine Phosphatase ◽  
Computational Study ◽  
Tyrosine Phosphatase ◽  
Receptor Kinase ◽  
Protein Tyrosine ◽  
Insulin Receptor Kinase ◽  
High Degree

The components and functions of the insulin receptor kinase signaling pathway have been conserved in a broad range of Metazoa ranging from mammals to insects and nematodes. There is a high degree of sequence homology and functional similarity between the human insulin receptor kinase (IRK) and the drosophila (Drosophila melanogaster) form (DIRK) of this enzyme. Similarly, a high degree of homology exists between human protein tyrosine phosphatase 1B (PTP1B) (which directly regulates IRK) and its drosophila counterpart DPTP61F (DPTP). However, genetic and biochemical studies have yet to demonstrate that DPTP61F acts in the DIRK pathway. Comparative structural modeling techniques using the known structures of human IRK and PTP1B as templates have yielded structures for the drosophila enzymes. The derived structures confirm that there is a high level of structural conservation at the tertiary level. Association of the DIRK and DPTP enzymes with each other was then investigated with a view to ascertaining whether DIRK might be a substrate of the DPTP. Evaluation of the interaction surfaces, including hydrophobic patch, shape, hydrogen bonding, and electrostatic compatibility, strongly suggested that the drosophila insulin receptor is a substrate of the DPTP. The interaction surfaces of the human and drosophila enzymes are structurally similar, although changes in critical residues modify possible electrostatic and hydrogen-bonding interactions. This suggests that in the mixed systems, DPTP–IRK or PTP1B–DIRK, the kinase domain will be a comparatively poor substrate for phosphatase activity when compared with the native systems.Key words: protein tyrosine phosphatase, insulin receptor kinase, Drosophila melanogaster, comparative protein modeling, surface topology, interaction zone.

Tissue localization of Drosophila melanogaster insulin receptor transcripts during development

1988 ◽  
Vol 8 (4) ◽  
pp. 1638-1647
Author(s):  
R S Garofalo ◽  
O M Rosen
Keyword(s):  
Nervous System ◽  
Drosophila Melanogaster ◽  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Protein Tyrosine Kinase ◽  
Kinase Activity ◽  
Ganglion Cells ◽  
Northern Analysis ◽  
Tyrosine Kinase Domain ◽  
Subunit Structure

The Drosophila melanogaster insulin receptor (Drosophila insulin receptor homolog [dIRH]) is similar to its mammalian counterpart in deduced amino acid sequence, subunit structure, and ligand-stimulated protein tyrosine kinase activity. The function of this receptor in D. melanogaster is not yet known. However, a role in development is suggested by the observations that levels of insulin-stimulated kinase activity and expression of dIRH mRNA are maximal during Drosophila midembryogenesis. In this study, a 2.9-kilobase (kb) cDNA clone corresponding to both the dIRH tyrosine kinase domain and some of the 3' untranslated sequence was used to determine the tissue distribution of dIRH mRNA during development. Two principal mRNAs of 11 and 8.6 kb hybridized with the dIRH cDNA in Northern (RNA) blot analysis. The abundance of the 8.6-kb mRNA increased transiently in early embryos, whereas the 11-kb species was most abundant during midembryogenesis. A similar pattern of expression was previously determined by Northern analysis, using a dIRH genomic clone (L. Petruzzelli, R. Herrera, R. Arenas-Garcia, R. Fernandez, M. J. Birnbaum, and O. M. Rosen, Proc. Natl. Acad. Sci. USA 83:4710-4714, 1986). In situ hybridization revealed dIRH transcripts in the ovaries of adult flies, in which the transcripts appeared to be synthesized by nurse cells for eventual storage as maternal RNA in the mature oocyte. Throughout embryogenesis, dIRH transcripts were ubiquitously expressed, although after midembryogenesis, higher levels were detected in the developing nervous system. Nervous system expression remained elevated throughout the larval stages and persisted in the adult, in which the cortex of the brain and ganglion cells were among the most prominently labeled tissues. In larvae, the imaginal disk cells exhibited comparatively high levels of dIRH mRNA expression. The broad distribution of dIRH mRNA in embryos and imaginal disks is compatible with a role for dIRH in anabolic processes required for cell growth. The apparently elevated expression of dIRH mRNA in nervous tissue during mid- and late embryogenesis coincides with a period of active neurite outgrowth and suggests that dIRH may be involved in this process.

Structure and ligand specificity of the Drosophila melanogaster insulin receptor

1987 ◽  
Vol 7 (8) ◽  
pp. 2718-2727
Author(s):  
R Fernandez-Almonacid ◽  
O M Rosen
Keyword(s):  
Amino Acids ◽  
Drosophila Melanogaster ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Insulin Binding ◽  
Beta Subunit ◽  
Evolutionary Divergence ◽  
Type I ◽  
Intact Cells ◽  
Antipeptide Antibody

The insulin-binding and protein tyrosine kinase subunits of the Drosophila melanogaster insulin receptor homolog have been identified and characterized by using antipeptide antibodies elicited to the deduced amino acid sequence of the alpha and beta subunits of the human insulin receptor. In D. melanogaster embryos and cell lines, the insulin receptor contains insulin-binding alpha subunits of 110 or 120 kilodaltons (kDa), a 95-kDa beta subunit that is phosphorylated on tyrosine in response to insulin in intact cells and in vitro, and a 170-kDa protein that may be an incompletely processed receptor. All of the components are synthesized from a proreceptor, joined by disulfide bonds, and exposed on the cell surface. The beta subunit is recognized by an antipeptide antibody elicited to amino acids 1142 to 1162 of the human insulin proreceptor, and the alpha subunit is recognized by an antipeptide antibody elicited to amino acids 702 to 723 of the human proreceptor. Of the polypeptide ligands tested, only insulin reacts with the D. melanogaster receptor. Insulinlike growth factors type I and II, epidermal growth factor, and the silkworm insulinlike prothoracicotropic hormone are unable to stimulate autophosphorylation. Thus despite the evolutionary divergence of vertebrates and invertebrates, the essential features of the structure and intrinsic functions of the insulin receptor have been remarkably conserved.

Impaired ovarian ecdysone synthesis of Drosophila melanogaster insulin receptor mutants

Aging Cell ◽  
2002 ◽  
Vol 1 (2) ◽  
pp. 158-160 ◽  
Author(s):  
Meng-Ping Tu ◽  
Chih-Ming Yin ◽  
Marc Tatar
Keyword(s):  
Drosophila Melanogaster ◽  
Insulin Receptor

scholarly journals Variation in morphological traits of Drosophila melanogaster (fruit fly) under nutritional stress

Heredity ◽  
1999 ◽  
Vol 82 (2) ◽  
pp. 187-192 ◽  
Author(s):  
Alexandra G Imasheva ◽  
Dmitri V Bosenko ◽  
Oleg A Bubli
Keyword(s):  
Drosophila Melanogaster ◽  
Morphological Traits ◽  
Fruit Fly ◽  
Nutritional Stress

scholarly journals Structure and ligand specificity of the Drosophila melanogaster insulin receptor.

1987 ◽  
Vol 7 (8) ◽  
pp. 2718-2727 ◽  
Author(s):  
R Fernandez-Almonacid ◽  
O M Rosen
Keyword(s):  
Amino Acids ◽  
Drosophila Melanogaster ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Insulin Binding ◽  
Beta Subunit ◽  
Evolutionary Divergence ◽  
Type I ◽  
Intact Cells ◽  
Antipeptide Antibody

The insulin-binding and protein tyrosine kinase subunits of the Drosophila melanogaster insulin receptor homolog have been identified and characterized by using antipeptide antibodies elicited to the deduced amino acid sequence of the alpha and beta subunits of the human insulin receptor. In D. melanogaster embryos and cell lines, the insulin receptor contains insulin-binding alpha subunits of 110 or 120 kilodaltons (kDa), a 95-kDa beta subunit that is phosphorylated on tyrosine in response to insulin in intact cells and in vitro, and a 170-kDa protein that may be an incompletely processed receptor. All of the components are synthesized from a proreceptor, joined by disulfide bonds, and exposed on the cell surface. The beta subunit is recognized by an antipeptide antibody elicited to amino acids 1142 to 1162 of the human insulin proreceptor, and the alpha subunit is recognized by an antipeptide antibody elicited to amino acids 702 to 723 of the human proreceptor. Of the polypeptide ligands tested, only insulin reacts with the D. melanogaster receptor. Insulinlike growth factors type I and II, epidermal growth factor, and the silkworm insulinlike prothoracicotropic hormone are unable to stimulate autophosphorylation. Thus despite the evolutionary divergence of vertebrates and invertebrates, the essential features of the structure and intrinsic functions of the insulin receptor have been remarkably conserved.

Author response for "Location and arrangement of campaniform sensilla in Drosophila melanogaster"

2020 ◽  
Author(s):  
Gesa F. Dinges ◽  
Alexander S. Chockley ◽  
Till Bockemühl ◽  
Kei Ito ◽  
Alexander Blanke ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Author Response ◽  
Campaniform Sensilla
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