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. Author manuscript; available in PMC: 2020 Jul 27.
Published in final edited form as: Lancet. 2015 Nov 3;387(10028):1657–1671. doi: 10.1016/S0140-6736(15)00728-X

Figure 3: Proteins affecting procollagen intracellular trafficking and extracellular crosslinking.

Figure 3:

Heat shock protein 47 is a specific collagen I chaperone, binding to the triple helical collagen domain in the endoplasmic reticulum, preventing aggregation, and facilitating its trafficking to the Golgi. An RDEL signal will then guide the return of heat shock protein 47 to the endoplasmic reticulum. FK506 binding protein 65 is a peptydyl prolyl cis-trans isomerase known to affect the activity of lysyl hydroxylase 2, the enzyme which hydroxylates lysine residues in the N-telopeptides and C-telopeptides that are crucial for crosslink formation in the extracellular matrix. The question marks refer to probable but not yet proven interactions.