Cell signaling by receptor tyrosine kinases.
Recent structural studies of receptor tyrosine kinases (RTKs) have revealed unexpected diversity in the mechanisms of their activation by growth factor ligands. Strategies for inducing dimerization by ligand binding are surprisingly diverse, as are mechanisms that couple this event to activation of the intracellular tyrosine kinase domains. As our understanding of these details becomes increasingly sophisticated, it provides an important context for therapeutically countering the effects of pathogenic RTK mutations in cancer and other diseases. Much remains to be learned, however, about the complex signaling networks downstream from RTKs and how alterations in these networks are translated into cellular responses.
Lemmon
Mark A
MA
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. mlemmon@mail.med.upenn.edu <mlemmon@mail.med.upenn.edu>
Schlessinger
Joseph
J
D000818:Animals; D004789:Enzyme Activation; D006801:Humans; D009369:Neoplasms / Q000188:drug therapy / Q000201:enzymology; D020794:Receptor Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D015398:Signal Transduction
D020794:Receptor Protein-Tyrosine Kinases