scholarly journals Independent signaling by Drosophila insulin receptor for axon guidance and growth

2014 ◽  
Vol 4 ◽  
Author(s):  
Caroline R. Li ◽  
Dongyu Guo ◽  
Leslie Pick
Keyword(s):  
Insulin Receptor ◽  
Axon Guidance ◽  
Drosophila Insulin Receptor

O-7: Drosophila insulin receptor function is required for normal growth

2009 ◽  
Vol 104 (S 02) ◽  
pp. 13-13
Author(s):  
Robert S. Garofalo ◽  
Chi Chen ◽  
Mireya Marin ◽  
Yimin Ruan ◽  
Joseph Jack
Keyword(s):  
Insulin Receptor ◽  
Normal Growth ◽  
Receptor Function ◽  
Drosophila Insulin Receptor

Membrane glycoproteins immunologically related to the human insulin receptor are associated with presumptive neuronal territories and developing neurones in Drosophila melanogaster

Development ◽  
1988 ◽  
Vol 103 (1) ◽  
pp. 145-156
Author(s):  
M. Piovant ◽  
P. Lena
Keyword(s):  
Nervous System ◽  
Insulin Receptor ◽  
Neuronal Differentiation ◽  
Human Insulin ◽  
Imaginal Discs ◽  
Membrane Glycoproteins ◽  
Western Blots ◽  
Molecular Pattern ◽  
Human Insulin Receptor ◽  
Drosophila Insulin Receptor

We have generated a monoclonal antibody (Mab E1C) that recognizes the differentiated nervous system in Drosophila embryos. At the cellular blastoderm stage, Mab E1C behaves as a general ectodermal marker but, in subsequent stages, it also labels the mesoderm. As neurogenesis takes place, staining increases within the neuromeres and is almost exclusively restricted to the nervous tissue by the time neuronal differentiation is completed. In third instar larvae, Mab E1C stains the central nervous system (CNS) as well as the imaginal discs which display a staining pattern related to their degree of neuronal differentiation. No labelling can be detected in adult brains or ovaries. Western blots are consistent with this developmental profile and allow the characterization of a major glycoprotein of 135 × 10(3) Mr (135K) which cosediments with a membrane fraction prepared from embryos. Additional glycoproteins (100K and 80K) are extracted from embryo homogenates by immunoaffinity procedures. In larvae, the 100K polypeptide is not detected. The properties of the 135K and 100K components are highly reminiscent of the molecular pattern of the Drosophila insulin receptor homologue (Petruzzelli et al. (1985) J. biol. Chem. 250, 16072–16075). It is shown that a Mab directed against the human insulin receptor stains the same cells as Mab E1C in imaginal discs and in the CNS. Moreover, this Mab cross-reacts with the 135K and 100K components of the embryonic antigen E1C.

scholarly journals The Drosophila insulin receptor activates multiple signaling pathways but requires insulin receptor substrate proteins for DNA synthesis.

1996 ◽  
Vol 16 (5) ◽  
pp. 2509-2517 ◽  
Author(s):  
L Yenush ◽  
R Fernandez ◽  
M G Myers ◽  
T C Grammer ◽  
X J Sun ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Tyrosine Phosphorylation ◽  
Human Insulin ◽  
Mammalian Cells ◽  
Insulin Response ◽  
Mitogen Activated Protein Kinase ◽  
Insulin Receptor Substrate ◽  
Human Insulin Receptor ◽  
Irs Proteins ◽  
Drosophila Insulin Receptor

The Drosophila insulin receptor (DIR) contains a 368-amino-acid COOH-terminal extension that contains several tyrosine phosphorylation sites in YXXM motifs. This extension is absent from the human insulin receptor but resembles a region in insulin receptor substrate (IRS) proteins which binds to the phosphatidylinositol (PI) 3-kinase and mediates mitogenesis. The function of a chimeric DIR containing the human insulin receptor binding domain (hDIR) was investigated in 32D cells, which contain few insulin receptors and no IRS proteins. Insulin stimulated tyrosine autophosphorylation of the human insulin receptor and hDIR, and both receptors mediated tyrosine phosphorylation of Shc and activated mitogen-activated protein kinase. IRS-1 was required by the human insulin receptor to activate PI 3-kinase and p70s6k, whereas hDIR associated with PI 3-kinase and activated p70s6k without IRS-1. However, both receptors required IRS-1 to mediate insulin-stimulated mitogenesis. These data demonstrate that the DIR possesses additional signaling capabilities compared with its mammalian counterpart but still requires IRS-1 for the complete insulin response in mammalian cells.

Characterization of the Drosophila insulin receptor promoter

2007 ◽  
Vol 1769 (4) ◽  
pp. 236-243 ◽  
Author(s):  
Sergio Casas-Tinto ◽  
Michael T. Marr ◽  
Pedro Andreu ◽  
Oscar Puig
Keyword(s):  
Insulin Receptor ◽  
Drosophila Insulin Receptor
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