Transforming growth factor (TGF)-β family proteins are synthesized as precursors that are
cleaved to generate an active ligand. Previous studies suggest that TGF-β activity can be
controlled by lysosomal degradation of both precursor proteins and ligands, but how these
soluble proteins are trafficked to the lysosome is incompletely understood. The current
studies show that sortilin selectively co-immunoprecipitates with the cleaved prodomain
and/or precursor form of TGF-β family members. Furthermore, sortilin co-localizes with, and …