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The protein tyrosine kinase group can be divided into two main groups: cytosolic tyrosine kinases (CTKs) or non-receptor tyrosine kinases (e.g. Src, JAK, Abl) and receptor tyrosine kinases (RTK). Receptor tyrosine kinases such as EGFR, VEGFR, FLT3 are transmembrane proteins that are activated by the binding of an extracellular ligand that transduces the signal to the cytoplasm by phosphorylating tyrosine residues on the receptors themselves (autophosphorylation) and on downstream signaling proteins. Since tyrosine kinases regulate many key processes including cell growth and survival a dysregulation has been found in the development and progression of a wide range of cancers.
Receptor tyrosine kinases are transmembrane glycoproteins that are activated by ligand-induced receptor dimerization following by an autophosphorylation of tyrosine residues in the cytoplasmic region and the release of the autoinhibited state of the tyrosine kinase domain. Based on their kinase domain sequence and the overall structure they can be classified into at least five subgroups. The class III RTK's are characterised by the presence of five to seven immunoglobulin-like domains and play an important role in haematopoiesis. Dysregulation of class III RTK's is linked to the pathogenesis of leukemia.
Cytosolic Tyrosine kinases
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