Receptor Tyrosine kinases

Protein Tyrosine Kinases:

Receptor PTKs are comprised of an extracellular ligand-binding domain, a single transmembrane domain, and a cytoplasmic portion containing the catalytic core, as well as regulatory sequences. A general mechanism for ligand-induced activation of receptor tyrosine kinases has been established (Lemmon and Schlessinger, 1994 ), in which ligand binding to the extracellular domain induces receptor dimerization. Receptor dimerization in turn leads to activation of the catalytic protein tyrosine kinase domain and to tyrosine autophosphorylation. Phosphorylation of tyrosine residues that leads to generation of docking sites for SH2 (Src homology 2) and PTB (phosphotyrosine binding) domains of adaptor proteins (Pawson and Scott, 1997 ).

• Lemmon MA, Schlessinger J. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem Sci 1994 Nov;19(11):459-63
• Pawson T, Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. Science. 1997 Dec 19;278(5346):2075-80.

• Kyriakis JM. Signaling by the germinal center kinase family of protein kinases. J Biol Chem. 1999 Feb 26;274(9):5259-62.