title: Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.
abstract: 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.
authors.affiliation: Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands.
authors.forename: Chantal
authors.initials: C
authors.lastname: Christis
authors.forename: Nicolette H
authors.initials: NH
authors.lastname: Lubsen
authors.forename: Ineke
authors.initials: I
authors.lastname: Braakman
mesh_terms: D051017:Apoptosis Regulatory Proteins / Q000502:physiology; D003600:Cytosol / Q000502:physiology*; D012321:DNA-Directed RNA Polymerases / Q000502:physiology; D003851:Deoxyribonucleases / Q000502:physiology; D019281:Dimerization; D004721:Endoplasmic Reticulum / Q000502:physiology*; D005914:Globins / Q000502:physiology; D006023:Glycoproteins / Q000502:physiology; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology*; D007075:Immunoglobulin M / Q000096:biosynthesis; D037102:Lectins / Q000502:physiology; D008562:Membrane Glycoproteins / Q000502:physiology; D018832:Molecular Chaperones / Q000502:physiology; D050862:Oxidoreductases Acting on Sulfur Group Donors; D019696:Peptidylprolyl Isomerase / Q000502:physiology; D011108:Polymers; D019704:Protein Disulfide-Isomerases / Q000502:physiology; D017510:Protein Folding; D021381:Protein Transport / Q000502:physiology; D011948:Receptors, Antigen, T-Cell / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology; D013954:Thyroglobulin / Q000096:biosynthesis; D038205:beta-Crystallin A Chain / Q000502:physiology
chemical_list: D051017:Apoptosis Regulatory Proteins; D006023:Glycoproteins; D018840:HSP70 Heat-Shock Proteins; D007075:Immunoglobulin M; D037102:Lectins; D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D011108:Polymers; D011948:Receptors, Antigen, T-Cell; D029701:Saccharomyces cerevisiae Proteins; D038205:beta-Crystallin A Chain; C109664:caspase-activated DNase inhibitor; C053387:endoplasmin; D005914:Globins; D013954:Thyroglobulin; D050862:Oxidoreductases Acting on Sulfur Group Donors; C113186:ERO1 protein, S cerevisiae; D012321:DNA-Directed RNA Polymerases; D003851:Deoxyribonucleases; C109663:caspase-activated deoxyribonuclease; D019696:Peptidylprolyl Isomerase; D019704:Protein Disulfide-Isomerases