fig1

Figure 1. Distinct structure and expression patterns of GDF8 and GDF11. GDF8 and GDF11 share 89% amino acid identity in their mature domain, but only 52% in their prodomain. During processing, the signal sequence (SS) is removed, and the pre-pro-ligands are cleaved by Furin and Tolloid proteases (TLDs) to prepare the mature ligand for future signaling. GDF8, expressed predominantly in skeletal muscle, is cleaved by all TLDs and preferentially by TLL2 due to the availability of this TLD in the muscle, while the ubiquitously expressed GDF11 is cleaved preferentially by BMP1 and TLL1^[6]. Figure made by @Biorender.