Human Discoidin Domain Receptor Family, Member 1 (DDR1) Protein

Background

Discoidin domain receptor 1 (DDR1) is a receptor tyrosine kinase (RTK) that uniquely binds to collagens, distinguishing it from other RTKs that are primarily activated by growth factors or hormones. DDR1 is encoded by the DDR1 gene located on chromosome 6p21.3 in humans and is widely expressed across various tissues, including the kidneys, brain, lungs, and reproductive organs. DDR1 has critical roles in cell adhesion, proliferation, migration, and differentiation, primarily through its unique capacity to interact with the extracellular matrix (ECM), particularly collagens. As a collagen-binding receptor, DDR1 is involved in cellular responses to structural changes in the ECM, making it essential in tissue remodeling, wound healing, and organ development. DDR1 has become increasingly significant in the context of cancer biology due to its involvement in cell adhesion and motility, which are critical for metastasis. It is also implicated in fibrotic diseases, where it contributes to tissue stiffness and fibrosis, and in immune response modulation. The discovery of DDR1 has broadened the understanding of RTKs, as it revealed a subset of kinases that function primarily through interactions with ECM proteins, underscoring its role in both physiological and pathological conditions.