| abstract |
Members of the collagen family are ligands for the discoidin domain receptor tyrosine kinases, DDR1 and DDR2. Collagen directly interacts with the extracellular domains and evokes tyrosine phosphorylation of DDRs in a time and concentration dependent manner. Collagen activation of DDR1 induced phosphorylation of a docking site for the Shc phosphotyrosine binding domain. Therefore, isolated complexes are described comprising (a) a discoidin domain receptor tyrosine kinase or a part thereof, and a collagen or a part thereof; or (b) a discoidin domain receptor tyrosine kinase or a part thereof and Shc or PTB binding domain of Shc or a protein containing a PDZ domain or a PDZ domain. Compositions, methods, and uses are also described based on the interaction of DDRs with collagens. |