The endoplasmic reticulum as a protein-folding compartment.

The lumen of the endoplasmic reticulum (ER) provides a dynamic and efficient environment for the folding of proteins destined for secretion and for a variety of cellular compartments and membranes. Usually, the folding process begins on the nascent chains and is completed minutes or hours later during assembly of oligomers. It is assisted by molecular chaperones and folding enzymes, some of which are unique to the ER. Quality control and selective degradation systems ensure only conformationally mature proteins are transported from the ER.

[1]  T. Hunter,et al.  Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport , 1991, The Journal of cell biology.

[2]  C. Zuker,et al.  The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins , 1991, Cell.

[3]  A. Helenius,et al.  Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum , 1992, Nature.

[4]  R. Pettersson,et al.  Formation and intracellular transport of a heterodimeric viral spike protein complex , 1991, The Journal of cell biology.

[5]  A Helenius,et al.  Folding of influenza hemagglutinin in the endoplasmic reticulum , 1991, The Journal of cell biology.

[6]  R. Freedman Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins , 1989, Cell.

[7]  H. Lodish,et al.  Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum. , 1991, The Journal of biological chemistry.

[8]  H. Scheraga,et al.  Experimental and theoretical aspects of protein folding. , 1975, Advances in protein chemistry.

[9]  K. Kivirikko,et al.  Post‐Translational Processing of Procollagens , 1985, Annals of the New York Academy of Sciences.

[10]  T. Creighton Disulfide bonds as probes of protein folding pathways. , 1986, Methods in enzymology.

[11]  J. Bonifacino,et al.  A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum. , 1990, Science.

[12]  P. H. Cameron,et al.  SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. , 1991, The Journal of biological chemistry.

[13]  H. Lodish,et al.  Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. , 1990, The Journal of biological chemistry.

[14]  A. Superti-Furga,et al.  Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase. , 1991, The Journal of biological chemistry.

[15]  L. Bergman,et al.  Formation of an intrachain disulfide bond on nascent immunoglobulin light chains. , 1979, The Journal of biological chemistry.

[16]  M. Rose,et al.  KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene , 1989, Cell.

[17]  H. Pelham Speculations on the functions of the major heat shock and glucose-regulated proteins , 1986, Cell.

[18]  F. Hartl,et al.  Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding , 1992, Nature.

[19]  J. Paulson,et al.  Glycoproteins: what are the sugar chains for? , 1989, Trends in biochemical sciences.

[20]  J. Bonifacino,et al.  Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP , 1991, The Journal of cell biology.

[21]  P. Arvan,et al.  Folding and assembly of newly synthesized thyroglobulin occurs in a pre-Golgi compartment. , 1991, The Journal of biological chemistry.

[22]  R. Mazzarella,et al.  ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. , 1990, The Journal of biological chemistry.

[23]  W. Lennarz,et al.  Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum. , 1992, The Journal of biological chemistry.

[24]  P. Rottier,et al.  An internalized amino-terminal signal sequence retains full activity in vivo but not in vitro. , 1987, The Journal of biological chemistry.

[25]  P. Silver,et al.  A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein , 1989, The Journal of cell biology.

[26]  A. S. Lee,et al.  Biochemical characterization of the 94- and 78-kilodalton glucose-regulated proteins in hamster fibroblasts. , 1984, The Journal of biological chemistry.

[27]  C. Alberini,et al.  Developmental regulation of IgM secretion: The role of the carboxy-terminal cysteine , 1990, Cell.

[28]  T. Peters,et al.  The biosynthesis of rat serum albumin. In vivo studies on the formation of the disulfide bonds. , 1982, The Journal of biological chemistry.

[29]  R. Mazzarella,et al.  ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). , 1987, The Journal of biological chemistry.

[30]  A. Helenius,et al.  Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum , 1992, The Journal of cell biology.

[31]  A. Helenius,et al.  Protein oligomerization in the endoplasmic reticulum. , 1989, Annual review of cell biology.

[32]  A. Helenius,et al.  Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. , 1992, The EMBO journal.

[33]  R. Freedman,et al.  Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes , 1988, Nature.

[34]  J. Kearney,et al.  Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein , 1987, The Journal of cell biology.

[35]  M. Rose,et al.  Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast , 1990, The Journal of cell biology.

[36]  J. Rothman Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells , 1989, Cell.

[37]  J. Sambrook,et al.  Protein folding in the cell , 1992, Nature.

[38]  R. Jaenicke,et al.  Protein folding: local structures, domains, subunits, and assemblies. , 1991, Biochemistry.

[39]  A. De Maio,et al.  Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94. , 1992, The Journal of biological chemistry.

[40]  M. Wabl,et al.  Immunoglobulin heavy chain binding protein , 1983, Nature.