Send to

Choose Destination
Biochim Biophys Acta. 2013 Nov;1833(11):2479-91. doi: 10.1016/j.bbamcr.2013.04.008. Epub 2013 Apr 18.

A molecular ensemble in the rER for procollagen maturation.

Author information

Research Department, Shriners Hospital for Children, Portland, OR 97239, USA.


Extracellular matrix (ECM) proteins create structural frameworks in tissues such as bone, skin, tendon and cartilage etc. These connective tissues play important roles in the development and homeostasis of organs. Collagen is the most abundant ECM protein and represents one third of all proteins in humans. The biosynthesis of ECM proteins occurs in the rough endoplasmic reticulum (rER). This review describes the current understanding of the biosynthesis and folding of procollagens, which are the precursor molecules of collagens, in the rER. Multiple folding enzymes and molecular chaperones are required for procollagen to establish specific posttranslational modifications, and facilitate folding and transport to the cell surface. Thus, this molecular ensemble in the rER contributes to ECM maturation and to the development and homeostasis of tissues. Mutations in this ensemble are likely candidates for connective tissue disorders. This article is part of a Special Issue entitled: Functional and structural diversity of endoplasmic reticulum.


Biosynthesis; Collagen; Endoplasmic reticulum; Extracellular matrix; Molecular chaperone; Posttranslational modification

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center