Reactome: A Curated Pathway Database

PDI is a chaperone for collagen peptides

Stable Identifier
R-HSA-2002460
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

As the collagen peptide chain is translocated across the membrane of the endoplasmic reticulum, intrachain disulfide bonds are formed within the N- and C-propeptides. This allows the triple helical domain to form a nucleation point at its C-terminal end and ensures correct alignment of the chains (Engel & Prockop 1991). Protein disulfide isomerase (P4HB) catalyzes the formation of both intra- (Bulleid & Freedman 1988) and inter-chain disulfide bonds (Koivu & Myllylä 1987). In addition, PDI acts as a molecular chaperone, interacting with monomeric collagen propeptide chains to prevent premature assembly or aggregation (Wilson et al. 1998).

Literature References
Participants
Participant Of
Orthologous Events