Comparative analysis of the signaling capabilities of the insulin receptor-related receptor

Although insulin receptor (InsR) and type I insulin-like growth factor receptor (IGF-IR) elicit different physiological effects in their target tissues, their signaling capabilities are similar to a large extent. In the present work, we investigated the potential of the third member of the family, i...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2005-02, Vol.327 (2), p.557-564
Main Authors: Klammt, Jürgen, Garten, Antje, Barnikol-Oettler, Anja, Beck-Sickinger, Annette G., Kiess, Wieland
Format: Article
Language:English
Subjects:
Humans
IGF-I receptor
Insulin receptor
IRR
Phosphorylation
Protein Binding
Protein Structure, Tertiary
Receptor, IGF Type 1 - metabolism
Receptor, Insulin - chemistry
Receptor, Insulin - genetics
Receptor, Insulin - metabolism
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Signal Transduction
Two-Hybrid System Techniques
Tyrosine phosphorylation
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Summary:Although insulin receptor (InsR) and type I insulin-like growth factor receptor (IGF-IR) elicit different physiological effects in their target tissues, their signaling capabilities are similar to a large extent. In the present work, we investigated the potential of the third member of the family, insulin receptor-related receptor (IRR), to associate with known interaction partners of the InsR and the IGF-I receptor in a yeast two-hybrid assay. Using the intracellular part of the IRR we found no association with any of the tested signaling molecules. Phosphotyrosine detection revealed a lack in the constitutive activation of the IRR described for analogous constructs of the two other members of the family. Replacement of the kinase domain of the IGF-IR or its C-terminal lobe alone into the IRR caused a complete restoration of the tyrosine phosphorylation of the IRR. The reestablishment of autophosphorylation was paralleled by restoration of interaction with a specific range of signaling molecules.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2004.12.039