Simultaneous induction of stimulatory and inhibitory signals by PDGF.
Platelet-derived growth factor (PDGF) exerts its effects on cells via binding to structurally similar alpha- and beta-tyrosine kinase receptors. Ligand binding induces receptor dimerization and autophosphorylation which allows docking of SH2 domain containing signal transduction molecules. At least 10 different SH2 domain molecules bind in a specific manner to 11 identified autophosphorylated tyrosine residues in the PDGF beta-receptor, thereby initiating signaling pathways leading to cell growth and motility. Available information indicates that there is considerable cross-talk between different signaling pathways, and that stimulatory and inhibitory signals often are initiated in parallel.
Heldin
C H
CH
Ludwig Institute for Cancer Research, Uppsala, Sweden.
D002455:Cell Division; D002633:Chemotaxis; D006801:Humans; D010982:Platelet-Derived Growth Factor / Q000378:metabolism*; D017479:Receptors, Platelet-Derived Growth Factor / Q000378:metabolism; D015398:Signal Transduction; D018909:src Homology Domains
D010982:Platelet-Derived Growth Factor; D017479:Receptors, Platelet-Derived Growth Factor