COL6A2 encodes the alpha-2 chain of collagen type VI, a critical extracellular matrix protein that forms trimeric complexes and acts as a cell-binding protein 1. The protein provides structural support to the extracellular matrix and exhibits cytoprotective functions, including inhibition of apoptosis and oxidative damage 1. COL6A2 mutations are among the most common causes of genetic neuromuscular disorders, with variants in the three COL6 genes (COL6A1, COL6A2, COL6A3) accounting for approximately 25% of identified muscle disease cases 2. These mutations cause a spectrum of congenital muscular disorders including Ullrich congenital muscular dystrophy, Bethlem myopathy, and myosclerosis myopathy, characterized by muscle wasting, weakness, joint contractures, and respiratory compromise 1. Glycine substitutions in the triple helical domain represent the most common pathogenic variants, with severity correlating to mutation position - the most severe cases cluster in triplets 10-15 of the N-terminal region 3. Beyond muscle pathology, COL6A2 dysfunction may contribute to satellite cell impairment, affecting muscle regeneration capacity 4. Recent evidence also suggests COL6A2 involvement in cancer biology, promoting tumor progression and immune evasion in glioblastoma 5.