Recepter Tyrosine Kinases

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Receptor tyrosine kinases activate tyrosine kinase enzymes which have intrinsic enzymatic activity, and is part of the receptor's polypeptide chain therefore encoded by the same gene[1]. It is the most common type of enzyme linked receptors, including insulin receptors and many growth factor receptors. Growth factor receptors control cell differentiation and proliferation, which is frequently associated with cancer.

Ligand binding to the extra-cellular domain induces the formation of receptor dimers - the process of two or more receptors joining together is known as 'activation by receptor oligomerization'[2]. Activated receptor chains autophosphorylate, which allows them to act as docking sites for other signalling proteins.

References

  1. Lodish H, Kaiser CA, Bretcher A, Amon A, Berk A, Kneger M, Ploegh H, Scott MP. Molecular Cell Biology. 7th Ed, New York: W.H. Freeman and Company. 2013.
  2. Lodish H, Kaiser CA, Bretcher A, Amon A, Berk A, Kneger M, Ploegh H, Scott MP. Molecular Cell Biology. 7th Ed, New York: W.H. Freeman and Company. 2013


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