Mature and active TGF-β ligands are formed by much larger precursor molecules. The active precursors include two of the carboxy-terminal mature domains in either homo- or heterodimer conformations. The amino-terminal signal peptide is cleaved at a conserved Arg-X-Arg-Arg site when translocated into the lumen of the rough endoplasmic reticulum, leaving the carboxy-terminal TGF-β superfamily mature monomer polypeptide. For TGF-β superfamily members, the mature domain is related to a latency associated peptide (LAP) which helps the protein move toward sites of activation or storage.
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