2. Recombinant Proteins
  3. Cytokines and Growth Factors Receptor Proteins Enzymes & Regulators
  4. PDGFs & PDGFRs Receptor Tyrosine Kinases Protein Tyrosine Kinases
  5. PDGFR

PDGFR

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Platelet-derived growth factor receptors (PDGFRs) belong to the receptor tyrosine kinase (RTK) family and serve the function of protein tyrosine kinases. PDGFRs are activated by binding to their ligand PDGFs, and involved in a variety of cellular processes, e.g. proliferation, migration, survival, and cancer development. PDGFRs are primarily located in vascular endothelial cells, fibroblasts and Kupffer cells. The two types of receptor, PDGFR-α and PDGFR-β, are structurally similar and consist of extracellular domains with five immunoglobulin (Ig) - like domains and intracellular parts with kinase domains which contain characteristic inserts of about 100 amino acid residues without homology to kinases. Ligand binding occurs mainly to Ig-like domains 2 and 3, and causes dimerization of the receptors, which is further stabilized by direct receptor-receptor interactions involving Ig-like domain 4.The dimerization is a key event in activation since it juxtaposes the intracellular parts promoting autophosphorylation in trans between the receptors. Subsequently, the phosphorylated PDGFR can initiate various downstream signaling events by recruiting SH2 domain-containing molecules such as Src kinase, Grb2, SHP2, PLCγ, Nck, and STAT.

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