Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Insulin Receptor

  • Antonio Brunetti
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_3076-3

Definition

IR is a phylogenetically ancient receptor tyrosine kinase protein embedded in the plasma membrane of virtually all cells. When the peptide hormone insulin binds to the IR, the receptor becomes activated and induces a cascade of intracellular events that will lead to several metabolic and growth-promoting effects.

Characteristics

The IR belongs to the tyrosine kinase growth factor receptor family and functions as an enzyme that transfers phosphate groups from ATP to tyrosine residues on intracellular target proteins. The IR consists of two identical extracellular alpha subunits (130 kDa) that house insulin binding domains and two transmembrane beta subunits (95 kDa) that contain ligand-activated tyrosine kinase activity in their intracellular domains (Fig. 1). When insulin binds to the alpha subunits, the receptor is first activated by tyrosine autophosphorylation, and then the IR tyrosine kinase phosphorylates various intracellular effector molecules (e.g., IRS proteins and...

Keywords

Insulin Resistance Tyrosine Kinase Growth Factor Neoplastic Breast Tissue Architectural Transcription Factor Direct Physical Association 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

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See Also

  1. (2012) AP2-alpha. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 230. doi:10.1007/978-3-642-16483-5_346Google Scholar
  2. (2012) ATP. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 302. doi:10.1007/978-3-642-16483-5_440Google Scholar
  3. (2012) Diabetes. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1105. doi:10.1007/978-3-642-16483-5_1601Google Scholar
  4. (2012) Glut4. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1559. doi:10.1007/978-3-642-16483-5_2435Google Scholar
  5. (2012) HMGA1. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1710. doi:10.1007/978-3-642-16483-5_2772Google Scholar
  6. (2012) Insulin. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, pp 1873–1874. doi:10.1007/978-3-642-16483-5_3075Google Scholar
  7. (2012) Insulin resistance. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1877. doi:10.1007/978-3-642-16483-5_3078Google Scholar
  8. (2012) IRS. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1917. doi:10.1007/978-3-642-16483-5_3150Google Scholar
  9. (2012) Obesity. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 2595. doi:10.1007/978-3-642-16483-5_4185Google Scholar
  10. (2012) Plasma membrane. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 2900. doi:10.1007/978-3-642-16483-5_4599Google Scholar
  11. (2012) SHC. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 3401. doi:10.1007/978-3-642-16483-5_5284Google Scholar
  12. (2012) TATA box. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, pp 3613–3614. doi:10.1007/978-3-642-16483-5_5682Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Department of Health SciencesUniversity of Catanzaro “Magna Græcia”CatanzaroItaly