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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Birnbaum, M. J. Petruzzelli, L. Fernandez, R. Herrera, R. Rosen, O. M. Arenas-garcia, R. |
| Abstract | A Drosophila genomic fragment has been isolated with a deduced amino acid sequence that is strikingly homologous to that of the kinase domain of the human insulin receptor. The Drosophila DNA hybridizes with an 11-kilobase mRNA that is most prominent in 8- to 12-hr embryos. An anti-peptide antibody prepared to a sequence in the human insulin receptor kinase domain that is conserved in the Drosophila sequence immunoprecipitates a single 95-kDa Drosophila protein whose phosphorylation on tyrosine residues is dependent on insulin. We conclude that the DNA sequence is that of the kinase domain of the Drosophila insulin receptor and that the 95-kDa phosphoprotein is the autophosphorylated beta subunit of that receptor. The results are compatible with our previous reports demonstrating a specific insulin-binding Drosophila glycoprotein and an insulin-dependent tyrosine protein kinase whose activity is greatest during embryogenesis. The observations suggest a role for insulin-dependent protein tyrosine phosphorylation during embryogenesis. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 13 |
| Volume Number | 83 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1986-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Drosophila Melanogaster Genetics Protein-Tyrosine Kinases Receptor, Insulin Amino Acid Sequence Animals Chromosome Mapping Cloning, Molecular DNA Restriction Enzymes Molecular Weight Phosphoproteins Immunology RNA, Messenger Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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