Protein folding and modification in the mammalian endoplasmic reticulum

Braakman, I. and Bulleid, N.J. (2011) Protein folding and modification in the mammalian endoplasmic reticulum. Annual Review of Biochemistry, 80(1), pp. 71-99. (doi: 10.1146/annurev-biochem-062209-093836)

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Analysis of the human genome reveals that approximately a third of all open reading frames code for proteins that enter the endoplasmic reticulum (ER), demonstrating the importance of this organelle for global protein maturation. The path taken by a polypeptide through the secretory pathway starts with its translocation across or into the ER membrane. It then must fold and be modified correctly in the ER before being transported via the Golgi apparatus to the cell surface or another destination. Being physically segregated from the cytosol means that the ER lumen has a distinct folding environment. It contains much of the machinery for fulfilling the task of protein production, including complex pathways for folding, assembly, modification, quality control, and recycling. Importantly, the compartmentalization means that several modifications that do not occur in the cytosol, such as glycosylation and extensive disulfide bond formation, can occur to secreted proteins to enhance their stability before their exposure to the extracellular milieu. How these various machineries interact during the normal pathway of folding and protein secretion is the subject of this review.

Item Type:Articles
Additional Information:ISBN:9780824308803
Glasgow Author(s) Enlighten ID:Bulleid, Professor Neil
Authors: Braakman, I., and Bulleid, N.J.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Annual Review of Biochemistry
ISSN (Online):1545-4509
Published Online:13 April 2011

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