Fig. 1
From: Targeting TGF-β signal transduction for fibrosis and cancer therapy
A schematic representation of TGF-β activation The pro-TGF-β synthesized in the rough endoplasmic reticulum becomes latent TGF-β when cleaved by the convertase furin in the Golgi complex. Then the LAP dimer binds to mature TGF-β noncovalently to form a small latent complex (SLC). Then, SLC generally binds to LTBP, forming LLC, while binds to GARP in Treg cells. SLC is anchored to ECM proteins, including fibronectin and fibrillin, via LTBP. Both LTBP and GARP play a direct role in anchoring TGF-β for traction-driven activation by integrins. With the help of αβ integrins and mechanical force, latent TGF-β becomes active and connects to the TβR complex to regulate transcription