tailieunhanh - Báo cáo khoa học: Protein folding includes oligomerization – examples from the endoplasmic reticulum and cytosol

A correct three-dimensional structure is a prerequisite for protein function-ality, and therefore for life. Thus, it is not surprising that our cells are packed with proteins that assist protein folding, the process in which the native three-dimensional structure is formed. | REVIEW ARTICLE Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol Chantal Christis1 Nicolette H. Lubsen2 and Ineke Braakman1 1 Cellular Protein Chemistry Bijvoet Center for Biomolecular Research Utrecht University The Netherlands 2 Biomolecular Chemistry Radboud University Nijmegen The Netherlands Keywords chaperone disulfide bond formation endoplasmic reticulum ERAD glycosylation lectin oligomerization protein folding quality control unfolded protein response Correspondence I. Braakman Cellular Protein Chemistry Faculty of Science Padualaan 8 3584 CH Utrecht The Netherlands Fax 31 30 254 0980 Tel 31 30 253 2759 2184 E-mail A correct three-dimensional structure is a prerequisite for protein functionality and therefore for life. Thus it is not surprising that our cells are packed with proteins that assist protein folding the process in which the native three-dimensional structure is formed. In general plasma membrane and secreted proteins as well as those residing in compartments along the endocytic and exocytic pathways fold and oligomerize in the endoplasmic reticulum. The proteins residing in the endoplasmic reticulum are specialized in the folding of this subset of proteins which renders this compartment a protein-folding factory. This review focuses on protein folding in the endoplasmic reticulum and discusses the challenge of oligomer formation in the endoplasmic reticulum as well as the cytosol. Present address MRC Laboratory of Molecular Biology Cambridge UK Received 1 April 2008 revised 12 June 2008 accepted 9 July 2008 doi What is protein folding During translation amino acids are coupled via peptide bonds to create a linear polypeptide chain. This chain adopts an energetically favorable conformation during which hydrophobic amino acids are buried on the inside of soluble proteins and hydrophilic residues are mostly found in solvent-accessible sites. During the .