dInR, insulin receptor, DIR, sprout, IR
Gene model reviewed during 5.47
Gene model reviewed during 5.55
The 2146aa InR proreceptor is processed into the 120kD α and 170kD β InR subunits. The 170kD β subunit is further processed into a 90kD β subunit and a 60kD free carboxyl polypeptide. The subunits assemble into mature InR receptors with the structure α2(β170)2 and α2(β90)2.
The α subunit of InR protein is derived from
proteolytic processing of the 280kD proreceptor.
The β subunit of InR protein is derived from
proteolytic processing of the 280kD proreceptor.
The 90kD β subunit of InR protein is derived
from proteolytic processing of the larger 170kD β subunit after removal
of a 60kD carboxy-terminal free peptide.
The free 60kD carboxy terminus of InR protein
is produced from the 170kD β subunit by proteolytic processing.
InR protein includes a novel 400aa carboxyl-terminal extension with putative binding sites for SH2-domain containing signalling proteins.
An antibody prepared against a part of the human insulin receptor peptide that is conserved in the Drosophila sequence reacts with a 95kD polypeptide in Drosophila which is presumed to be an autophosphorylated β subunit of the receptor.
Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain. When autophosphorylated, the beta-subunit binds the SH2 and SH3 domains of the adapter protein Dock. The beta subunit also binds and tyrosine phosphorylates the insulin receptor substrate Chico.
The 280 kDa proreceptor is proteolytically processed to form a 120 kDa alpha subunit and a 170 kDa beta subunit. The beta subunit undergoes cell-specific cleavage to generate a 90 kDa beta subunit and a free 60 kDa C-terminal subunit. Both the 90 kDa and the 170 kDa beta subunits can assemble with the alpha subunits to form mature receptors.
Autophosphorylated on tyrosine residues in response to exogenous insulin.
Phosphorylation of Tyr-1354 is required for Chico-binding.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\InR using the Feature Mapper tool.
InR protein is abundant and widely distributed from the beginning of cellularization to the onset of gastrulation. It is found in all three germ layers in stage 9-11 embryos. It is particularly prominent in the posterior midgut primordium, epidermis and neuroblasts. By stage 12, strong expression is seen in the epidermis, the midgut, the hindgut, and in a segmentally repeated pattern in the ventral cord. In late embryonic stages, staining persists in both cell bodies and axons along the ventral nerve cord and in the supraoesophageal ganglion.
GBrowse - Visual display of RNA-Seq signalsView Dmel\InR in GBrowse 2
Maps to 3R.
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
InR plays an important role in spermatogenesis, by stimulating germline stem cell proliferation and spermatocyte growth.
When dsRNA constructs are made and transiently transfected into S2 cells in RNAi experiments, a decrease in the ratio of cells in prometaphase and metaphase versus the total number of mitotic cells is seen.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
Phylogenetic analysis of the PTK family.
InR has been cloned, primary structure determined, functional expression of the predicted polypeptide analysed and mutations isolated. Loss of function mutations cause pleiotropic recessive phenotypes that lead to embryonic lethality. InR activity is required in the embryonic epidermis and nervous system.
Chimeric receptors containing either all or a portion of the cytoplasmic domain of Drosophila InR are indistinguishable from the human insulin receptor in terms of signalling when transfected into COS-7 or CHO cells.
InR carboxy terminus undergoes a conformational change during the activation-inactivation cycle of the kinase which can be sterically hindered by an antipeptide antibody against the carboxy terminus. Conformational changes have also been observed in the mammalian insulin receptor.
The temporal and spatial restriction of the InR protein to the developing neuromuscular junction suggests that it might be involved in the expansion and maturation of motor innervation during larval growth.
A specific high affinity insulin binding protein, a membrane associated glycoprotein with an Mr of 300,000 to 400,000, has been found that binds bovine and porcine insulin.
High affinity insulin binding and insulin-dependent protein tyrosine kinase activity are found in membranes.
Insulin-dependent protein tyrosine kinase activity is differentially expressed during development, peaks during embryogenesis, suggesting that insulin may be involved in tissue and organ differentiation during embryogenesis.