DDR1 is a collagen-binding receptor tyrosine kinase that serves as a key sensor of extracellular matrix (ECM) composition and state 1. Upon collagen binding, DDR1 activates signaling cascades involving autophosphorylation and downstream kinases to regulate cell adhesion, migration, differentiation, and matrix remodeling 2. DDR1 upregulates matrix metalloproteinases (MMP2, MMP7, MMP9) to facilitate ECM remodeling and promote wound healing in normal physiology. In disease contexts, DDR1 dysregulation contributes to multiple pathologies. In vitiligo, reduced DDR1 expression compromises melanocyte-epithelial adhesion, facilitating autoimmune attack 3. In cancer, DDR1 plays multifaceted roles: it promotes immune exclusion by organizing collagen fiber alignment, obstructing T cell infiltration in triple-negative breast cancer 4; regulates tumor metabolism through collagen-dependent macropinocytosis 1; and drives gastric cancer progression via the DDR1-HIF-1α axis, enhancing angiogenesis and metastatic capacity 5. DDR1 expression correlates with an immune-exclusion signature in colorectal cancer progression 6. Clinically, DDR1 represents a therapeutic target for cancer, fibrosis, atherosclerosis, and neurodegenerative diseases 7. DDR1 inhibitors show promise in preclinical models 8, though drug development faces challenges including selectivity and complex ECM interactions.