Recepter Tyrosine Kinases: Difference between revisions
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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<ref>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.</ref>. 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. | Receptor tyrosine kinases activate tyrosine kinase [[enzymes|enzymes]] which have [[intrinsic enzymatic activity|intrinsic enzymatic activity]], and is part of the receptor's [[polypeptide chain|polypeptide chain]] therefore encoded by the same [[gene|gene]]<ref>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.</ref>. It is the most common type of enzyme linked receptors, including [[insulin receptor|insulin receptors]] and many [[growth factor receptor|growth factor receptors]]. Growth factor receptors control [[cell differentiation|cell differentiation]] and [[cell proliferation|proliferation]], which is frequently associated with [[cancer|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'<ref>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</ref>. Activated receptor chains autophosphorylate, which allows them to act as docking sites for other signalling proteins. | 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'<ref>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</ref>. Activated receptor chains [[Autophosphorylate|autophosphorylate]], which allows them to act as docking sites for other signalling proteins.<br> | ||
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Latest revision as of 17:51, 4 December 2017
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
- ↑ 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.
- ↑ 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