Versatility of the endoplasmic reticulum protein folding factory

Critical Reviews in Biochemistry and Molecular Biology

Volumn 40, Issue 4, 2005, Pages 191-228

  Van Anken, Eelco ^a   Braakman, Ineke ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

Author keywords

BiP; Calnexin; Chaperones; EDEM; ERAD; PDI

Indexed keywords

CALNEXIN; CHAPERONE; GLUCOSE REGULATED PROTEIN 78;

DISULFIDE BOND; ENDOPLASMIC RETICULUM; EUKARYOTIC CELL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; PROTEIN SYNTHESIS; REVIEW;

ENDOPLASMIC RETICULUM; GLYCOPROTEINS; GLYCOSYLATION; HYDROPHOBICITY; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; PROTEIN DENATURATION; PROTEIN FOLDING; QUALITY CONTROL; SIGNAL TRANSDUCTION; UBIQUITIN;

EUKARYOTA;

EID: 23744457478     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.1080/10409230591008161     Document Type: Review

References (450)

1. Abeijon, C. and Hirschberg, C.B. 1992. Topography of glycosylation reactions in the endoplasmic reticulum. Trends Biochem Sci 17:32-36.
2. Abell, B.M., Jung, M., Oliver, J.D., Knight, B.C., Tyedmers, J., Zimmermann, R., and High, S. 2003. Tail-anchored and signal-anchored proteins utilize overlapping pathways during membrane insertion. J Biol Chem 278:5669-5678.
3. Alanen, H.I., Williamson, R.A., Howard, M.J., Lappi, A.K., Jantti, H.P., Rautio, S.M., Kellokumpu, S., and Ruddock, L.W. 2003. Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member. J Biol Chem 278:28912-28920.
4. Alder, N.N., Shen, Y., Brodsky, J.L., Hendershot, L.M., and Johnson, A.E. 2005. The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. J Cell Biol 168:389-399.
5. Allen, S., Naim, H.Y., and Bulleid, N.J. 1995. Intracellular folding of tissue-type plasminogen activator. Effects of disulfide bond formation on N-linked glycosylation and secretion. J Biol Chem 270:4797-4804.
6. Anelli, T., Alessio, M., Bachi, A., Bergamelli, L., Bertoli, G., Camerini, S., Mezghrani, A., Ruffato, E., Simmen, T., and Sitia, R. 2003. Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44. Embo J 22:5015-5022.
7. Anelli, T., Alessio, M., Mezghrani, A., Simmen, T., Talamo, F., Bachi, A., and Sitia, R. 2002. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. Embo J 21:835-844.
8. Anfinsen, C.B. and Scheraga, H.A. 1975. Experimental and theoretical aspects of protein folding. Adv Protein Chem 29:205-300.
9. Antoniou, A.N., Ford, S., Alphey, M., Osborne, A., Elliott, T., and Powis, S.J. 2002. The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules. Embo J 21:2655-2663.
10. Appenzeller, C., Andersson, H., Kappeler, F., and Hauri, H.P. 1999. The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nat Cell Biol 1:330-334.
11. Arber, S., Krause, K.H., and Caroni, P. 1992. s-cyclophilin is retained Intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin. J Cell Biol 116:113-125.
12. Argon, Y. and Simen, B.B. 1999. GRP94, an ER chaperone with protein and peptide binding properties. Semin Cell Dev Biol 10:495-505.
13. Atkinson, P.H. and Lee, J.T. 1984. Co-translational excision of alpha-glucose and alpha-mannose in nascent vesicular stomatitis virus G protein. J Cell Biol 98:2245-2249.
14. Bakos, E., Evers, R., Szakacs, G., Tusnady, G.E., Welker, E., Szabo, K., De Haas, M., Van Deemter, L., Borst, P., Varadi, A., et al. 1998. Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain. J Biol Chem 273:32167-32175.
15. Bando, Y., Ogawa, S., Yamauchi, A., Kuwabara, K., Ozawa, K., Hori, O., Yanagi, H., Tamatani, M., and Tohyama, M. 2000. 150-kDa oxygen-regulated protein (ORP150) functions as a novel molecular chaperone in MDCK cells. Am J Physiol Cell Physiol 278:C1172-C1182.
16. Bardwell, J.C., Mcgovern, K., and Beckwith, J. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-589.
17. Baxter, B.K., James, P., Evans, T., and Craig, E.A. 1996. SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum. Mol Cell Biol 16:6444-6456.
18. Bays, N.W., Gardner, R.G., Seelig, L.P., Joazeiro, C.A., and Hampton, R.Y. 2001. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol 3:24-29.
19. Belden, W.J. and Barlowe, C. 2001. Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles. Science 294:1528-1531.
20. Benham, A.M., Cabibbo, A., Fassio, A., Bulleid, N., Sitia, R., and Braakman, I. 2000. The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha. Embo J 19:4493-4502.
21. Berchtold, M.W., Brinkmeier, H., and Muntener, M. 2000. Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity, and disease. Physiol Rev 80:1215-1265.
22. Biederer, T., Volkwein, C., and Sommer, T. 1997. Role of Cuelpin ubiquitination and degradation at the ER surface. Science 278:1806-1809.
23. Blobel, G. and Dobberstein, B. 1975. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol 67:835-851.
24. Blom, D., Hirsch, C., Stern, P., Tortorella, D., and Ploegh, H.L. 2004. A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised. Embo J 23:650-658.
25. Boisrame, A., Kabani, M., Beckerich, J.M., Hartmann, E., and Gaillardin, C. 1998. Interaction of Kar2p and SIs1p is required for efficient cotranslational translocation of secreted proteins in the yeast Yarrowia lipolytica. J Biol Chem 273:30903-30908.
26. Bordallo, J., Plemper, R.K., Finger, A., and Wolf, D.H. 1998. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol Biol Cell 9:209-222.
27. Borel, A.C. and Simon, S.M. 1996. Biogenesis of polytopic membrane proteins: membrane segments assemble within translocation channels prior to membrane integration. Cell 85:379-389.
28. Braakman, I. 2001. A novel lectin in the secretory pathway. An elegant mechanism for glycoprotein elimination. EMBO Rep 2:666-668.
29. Braakman, I., Helenius, J., and Helenius, A. 1992a. Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. Embo J 11:1717-1722.
30. Braakman, I., Helenius, J., and Helenius, A. 1992b. Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 356:260-262.
31. Braakman, I., Hoover-Litty, H., Wagner, K.R., and Helenius, A. 1991. Folding of influenza hemagglutinin in the endoplasmic reticulum. J Cell Biol 114:401-411.
32. Brightman, S.E., Blatch, G.L., and Zetter, B.R. 1995. Isolation of a mouse cDNA encoding MTJ1, a new murine member of the DnaJ family of proteins. Gene 153:249-254.
33. Brodsky, J.L., Werner, E.D., Dubas, M.E., Goeckeler, J.L., Kruse, K.B., and Mccracken, A.A. 1999. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J Biol Chem 274:3453-3460.
34. Brostrom, M.A. and Brostrom, C.O. 2003. Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability. Cell Calcium 34:345-363.
35. Bryngelson, J.D., Onuchic, J.N., Socci, N.D., and Wolynes, P.G. 1995. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 21:167-195.
36. Bu, G. 2001. The roles of receptor-associated protein (RAP) as a molecular chaperone for members of the LDL receptor family. Int Rev Cytol 209:79-116.
37. Bu, G., Geuze, H.J., Strous, G.J., and Schwartz, A.L. 1995. 39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein. Embo J 14:2269-2280.
38. Buck, T.M. and Skach, W.R. 2005. Differential stability of biogenesis intermediates reveals a common pathway for aquaporin-1 topological maturation. J Biol Chem 280:261-269.
39. Bukau, B. and Horwich, A.L. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366.
40. Bulleid, N.J. and Freedman, R.B. 1988. Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature 335:649-651.
41. Cabibbo, A., Pagani, M., Fabbri, M., Rocchi, M., Farmery, M.R., Bulleid, N.J., and Sitia, R. 2000. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem 275:4827-4833.
42. Cabral, C.M., Liu, Y., and Sifers, R.N. 2001. Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem Sci 26:619-624.
43. Caldwell, S.R., Hill, K.J., and Cooper, A.A. 2001. Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi. J Biol Chem 276:23296-23303.
44. Cannon, K.S. and Cresswell, P. 2001. Quality control of transmembrane domain assembly in the tetraspanin CD82. Embo J 20:2443-2453.
45. Chakravarthi, S. and Bulleid, N.J. 2004. Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway. J Biol Chem 279:39872-39879.
46. Chang, T.S. and Morton, B. 1975. Epididymal sulfhydryl oxidase: a sperm-protective enzyme from the male reproductive tract. Biochem Biophys Res Commun 66:309-315.
47. Chaudhuri, M.M., Tonin, P.N., Lewis, W.H., and Srinivasan, PR. 1992. The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells. Biochem J 281:645-650.
48. Chen, W. and Helenius, A. 2000. Role of ribosome and translocon complex during folding of influenza hemagglutinin in the endoplasmic reticulum of living cells. Mol Biol Cell 11:765-772.
49. Chen, X., Easton, D., Oh, H.J., Lee-Yoon, D.S., Liu, X., and Subjeck, J. 1996. The 170 kDa glucose regulated stress protein is a large HSP70-, HSP110-like protein of the endoplasmic reticulum. FEBS Lett 380:68-72.
50. Chung, K.T., Shen, Y., and Hendershot, L.M. 2002. BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. J Biol Chem 277:47557-47563.
51. Clemons, W.M., Jr., Menetret, J.F., Akey, C.W., and Rapoport, T.A. 2004. Structural insight into the protein translocation channel. Curr Opin Struct Biol 14:390-396.
52. Coppock, D.L., Cina-Poppe, D., and Gilleran, S. 1998. The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1. Genomics 54:460-468.
53. Corbett, E.F., Oikawa, K., Francois, P., Tessier, D.C., Kay, C., Bergeron, J.J., Thomas, D.Y., Krause, K.H., and Michalak, M. 1999. Ca2+ regulation of interactions between endoplasmic reticulum chaperones. J Biol Chem 274:6203-6211.
54. Craven, R.A., Egerton, M., and Stirling, C.J. 1996. A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors. Embo J 15:2640-2650.
55. Cunnea, P.M., Miranda-Vizuete, A., Bertoli, G., Simmen, T., Damdimopoulos, A.E., Hermann, S., Leinonen, S., Huikko, M.P., Gustafsson, J.A., Sitia, R., et al. 2003. ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. J Biol Chem 278:1059-1066.
56. Daggett, V. and Fersht, A. 2003. The present view of the mechanism of protein folding. Nat Rev Mol Cell Biol 4:497-502.
57. Daniels, R., Kurowski, B., Johnson, A.E., and Hebert, D.N. 2003. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol Cell 11:79-90.
58. Das, A.T., Land, A., Braakman, I., Klaver, B., and Berkhout, B. 1999. HIV-1 evolves into a nonsyncytium-inducing virus upon prolonged culture in vitro. Virology 263:55-69.
59. De Kroon, A.I., Koorengevel, M.C., Vromans, T.A., and DeKruijff, B. 2003. Continuous equilibration of phosphatidylcholine and its precursors between endoplasmicreticulum and mitochondria in yeast. Mol Biol Cell 14:2142-2150.
60. De Virgilio, M., Kitzmuller, C., Schwaiger, E., Klein, M., Kreibich, G., and Ivessa, N.E. 1999. Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response. Mol Biol Cell 10:4059-4073.
61. Demmer, J., Zhou, C., and Hubbard, M.J. 1997. Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum. FEBS Lett 402:145-150.
62. Denzel, A., Molinari, M., Trigueros, C., Martin, J.E., Velmurgan, S., Brown, S., Stamp, G., and Owen, M.J. 2002. Early postnatal death and motor disorders in mice congenially deficient in calnexin expression. Mol Cell Biol 22:7398-7404.
63. Desilva, M.G., Lu, J., Donadel, G., Modi, W.S., Xie, H., Notkins, A.L., and Lan, M.S. 1996. Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas. DNA Cell Biol 15:9-16.
64. Dierks, T., Volkmer, J., Schlenstedt, G., Jung, C., Sandholzer, U., Zachmann, K., Schlotterhose, P., Neifer, K., Schmidt, B., and Zimmermann, R. 1996. A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum. Embo J 15:6931-6942.
65. Do, H., Falcone, D., Lin, J., Andrews, D.W., and Johnson, A.E. 1996. The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 85:369-378.
66. Dobson, C.M. 2003. Protein folding and disease: a view from the first Horizon Symposium. Nat Rev Drug Discov 2:154-160.
67. Dudek, J., Volkmer, J., Bies, C., Guth, S., Muller, A., Lerner, M., Feick, P., Schafer, K.H., Morgenstern, E., Hennessy, F., et al. 2002. A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes. Embo J 21:2958-2967.
68. Easton, D.P., Kaneko, Y., and Subjeck, J.R. 2000. The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress Chaperones 5:276-290.
69. Egea, P.F., Shan, S.O., Napetschnig, J., Savage, D.F., Walter, P., and Stroud, R.M. 2004. Substrate twinning activates the signal recognition particle and its receptor. Nature 427:215-221.
70. Elbein, A.D. 1991. Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing. Faseb J 5:3055-3063.
71. Ellgaard, L., Molinari, M., and Helenius, A. 1999. Setting the standards: quality control in the secretory pathway. Science 286:1882-1888.
72. Ellgaard, L. and Helenius, A. 2003. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4:181-191.
73. Ellgaard, L., Riek, R., Herrmann, T., Guntert, P., Braun, D., Helenius, A., and Wuthrich, K. 2001. NMR structure of the calreticulin P-domain. Proc Natl Acad Sci U S A 98:3133-3138.
74. Ellgaard, L. and Ruddock, L.W. 2005. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep 6:28-32.
75. Ellis, R.J. and Hemmingsen, S.M. 1989. Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem Sci 14:339-342.
76. Epstein, C.J., Goldenberger, R.F., and Anfinsen, C.B. 1963. The genetic control of tertiary protein structure: studies with model systems. Cold Spring Harbor Symp. Quant Biol. 28:439-449.
77. Fagioli, C., Mezghrani, A., and Sitia, R. 2001. Reduction of interchain disulfide bonds precedes the dislocation of Ig-mu chains from the endoplasmic reticulum to the cytosol for proteasomal degradation. J Biol Chem 276:40962-40967.
78. Farquhar, R., Honey, N., Murant, S.J., Bossier, P., Schultz, L., Montgomery, D., Ellis, R.W., Freedman, R.B., and Tuite, M.F. 1991. Protein disulfide isomerase is essential for viability in Saccharomycescerevisiae. Gene 108:81-89.
79. Fassio, A. and Sitia, R. 2002. Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum. Histochem Cell Biol 117:151-157.
80. Feldheim, D., Rothblatt, J., and Schekman, R. 1992. Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol Cell Biol 12:3288-3296.
81. Fenouillet, E., Gluckman, J.C., and Jones, I.M. 1994. Functions of HIV envelope glycans. Trends Biochem Sci 19:65-70.
82. Fenton, W.A. and Horwich, A.L. 2003. Chaperonin-mediated protein folding: fate of substrate polypeptide. Q Rev Biophys 36:229-256.
83. Ferrari, D.M., Nguyen Van, P., Kratzin, H.D., and Soling, H.D. 1998. ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif. Eur J Biochem 255:570-579.
84. Ferrari, D.M. and Soling, H.D. 1999. The protein disulphide-isomerase family: unravelling a string of folds. Biochem J 339:1-10.
85. Ferreira, L.R., Norris, K., Smith, T., Hebert, C., and Sauk, J.J. 1994. Association of Hsp47, Grp78, and Grp94 with procollagen supports the successive or coupled action of molecular chaperones. J Cell Biochem 56:518-526.
86. Fiebiger, E., Story, C., Ploegh, H.L., and Tortorella, D. 2002. Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein. Embo J 21:1041-1053.
87. Flynn, G.C., Pohl, J., Flocco, M.T., and Rothman, J.E. 1991. Peptide-binding specificity of the molecular chaperone BiP. Nature 353:726-730.
88. Focia, P.J., Shepotinovskaya, I.V., Seidler, J.A., and Freymann, D.M. 2004. Heterodimeric GTPase core of the SRP targeting complex. Science 303:373-377.
89. Frand, A.R., Cuozzo, J.W., and Kaiser, C.A. 2000. Pathways for protein disulphide bond formation. Trends Cell Biol 10:203-210.
90. Frand, A.R. and Kaiser, C.A. 1999. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4:469-477.
91. Freedman, R.B., Hirst, T.R., and Tuite, M.F. 1994. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem Sci 19:331-336.
92. Frenkel, Z., Gregory, W., Kornfeld, S., and Lederkremer, G.Z. 2003. Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2. J Biol Chem 278:34119-34124.
93. Frenkel, Z., Shenkman, M., Kondratyev, M., and Lederkremer, G.Z. 2004. Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains. Mol Biol Cell 15:2133-2142.
94. Frickel, E.M., Riek, R., Jelesarov, I., Helenius, A., Wuthrich, K., and Ellgaard, L. 2002. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc Natl Acad Sci U S A 99:1954-1959.
95. Friedlander, R., Jarosch, E., Urban, J., Volkwein, C., and Sommer, T. 2000. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2:379-384.
96. Frigerio, G. and Pelham, H.R. 1993. A Saccharomyces cerevisiae cyclophilin resident in the endoplasmic reticulum. J Mol Biol 233:183-188.
97. Frydman, J. and Hohfeld, J. 1997. Chaperones get in touch: the Hip-Hop connection. Trends Biochem Sci 22:87-92.
98. Fullekrug, J., Sonnichsen, B., Wunsch, U., Arseven, K., Nguyen Van, P., Soling, H.D., and Mieskes, G. 1994. CaBP1, a calcium binding protein of the thioredoxin family, is a resident KDEL protein of the ER and not of the intermediate compartment. J Cell Sci 107:2719-2727.
99. Furman, M.H. and Ploegh, H.L. 2002. Lessons from viral manipulation of protein disposal pathways. J Clin Invest 110:875-879.
100. Galat, A. 2003. Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity-targets-functions. Curr Top Med Chem 3:1315-1347.
101. Gardner, R.G., Swarbrick, G.M., Bays, N.W., Cronin, S.R., Wilhovsky, S., Seelig, L., Kim, C., and Hampton, R.Y. 2000. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p. J Cell Biol 151:69-82.
102. Gerber, J., Muhlenhoff, U., Hofhaus, G., Lill, R., and Lisowsky, T. 2001. Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family. J Biol Chem 276:23486-23491.
103. Gething, M.J. 1999. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 10:465-472.
104. Gething, M.J. and Sambrook, J. 1992. Protein folding in the cell. Nature 355:33-45.
105. Geuze, H.J., Murk, J.L., Stroobants, A.K., Griffith, J.M., Kleijmeer, M.J., Koster, A.J., Verkleij, A.J., Distel, B., and Tabak, H.F. 2003. Involvement of the endoplasmic reticulum in peroxisome formation. Mol Biol Cell 14:2900-2907.
106. Ghaemmaghami, S., Huh, W.K., Bower, K., Howson, R.W., Belle, A., Dephoure, N., O'shea, E.K., and Weissman, J.S. 2003. Global analysis of protein expression in yeast. Nature 425:737-741.
107. Gillece, P., Luz, J.M., Lennarz, W.J., De La Cruz, F.J., and Romisch, K. 1999. Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J Cell Biol 147:1443-1456.
108. Gilmore, R., Blobel, G., and Walter, P. 1982a. Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J Cell Biol 95:463-469.
109. Gilmore, R., Walter, P., and Blobel, G. 1982b. Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor. J Cell Biol 95:470-477.
110. Gnann, A., Riordan, J.R., and Wolf, D.H. 2004. Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast. Mol Biol Cell 15:4125-4135.
111. Goder, V., Bieri, C., and Spiess, M. 1999. Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon J Cell Biol 147:257-266.
112. Goder, V., Junne, T., and Spiess, M. 2004. Sec61p contributes to signal sequence orientation according to the positive-inside rule. Mol Biol Cell 15:1470-1478.
113. Goder, V. and Spiess, M. 2001. Topogenesis of membrane proteins: determinants and dynamics. FEBS Lett 504:87-93.
114. Goder, V. and Spiess, M. 2003. Molecular mechanism of signal sequence orientation in the endoplasmic reticulum. Embo J 22:3645-3653.
115. Goldenberger, R.F., Epstein, C.J., and Anfinsen, C.B. 1963. Acceleration of reactivation of reduced bovine panreatic ribonuclease by a microsomal system from rat liver. J Biol Chem 238:628-635.
116. Gross, E., Kastner, D.B., Kaiser, C.A., and Fass, D. 2004. Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. Cell 117:601-610.
117. Gross, E., Sevier, C.S., Vala, A., Kaiser, C.A., and Fass, D. 2002. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat Struct Biol 9:61-67.
118. Haas, I.G. and Wabl, M. 1983. Immunoglobulin heavy chain binding protein. Nature 306:387-389.
119. Haigh, N.G. and Johnson, A.E. 2002. A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membrane. J Cell Biol 156:261-270.
120. Hamilton, T.G. and Flynn, G.C. 1996. Cer1p, a novel Hsp70-related protein required for posttranslational endoplasmic reticulum translocation in yeast. J Biol Chem 271:30610-30613.
121. Hamman, B.D., Hendershot, L.M., and Johnson, A.E. 1998. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92:747-758.
122. Hammond, C., Braakman, I., and Helenius, A. 1994. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci U S A 91:913-917.
123. Hammond, C. and Helenius, A. 1994. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266:456-458.
124. Hanein, D., Matlack, K.E., Jungnickel, B., Plath, K., Kalles, K.U., Miller, K.R., Rapoport, T.A., and Akey, C.W. 1996. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell 87:721-732.
125. Harding, H.P., Zhang, Y., Zeng, H., Novoa, I., Lu, P.D., Calfon, M., Sadri, N., Yun, C., Popko, B., Paules, R., et al. 2003. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 11:619-633.
126. Hartmann-Petersen, R., Seeger, M., and Gordon, C. 2003. Transferring substrates to the 26S proteasome. Trends Biochem Sci 28:26-31.
127. Hasel, K.W., Glass, J.R., Godbout, M., and Sutcliffe, J.G. 1991. An endoplasmic reticulum-specific cyclophilin. Mol Cell Biol 11:3484-3491.
128. Haugstetter, J., Blicher, T., and Ellgaard, L. 2005. Identification and characterization of a novel thioredoxin-related transmembrane protein of the endoplasmic reticulum. J Biol Chem 280:8371-8380.
129. Hawkins, H.C., De Nardi, M., and Freedman, R.B. 1991. Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase. Biochem J 275:341-348.
130. Hayano, T. and Kikuchi, M. 1995a. Cloning and sequencing of the cDNA encoding human P5. Gene 164:377-378.
131. Hayano, T. and Kikuchi, M. 1995b. Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR). FEBS Lett 372:210-214.
132. Haynes, C.M., Caldwell, S., and Cooper, A.A. 2002. An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J Cell Biol 158:91-101.
133. Haynes, C.M., Titus, E.A., and Cooper, A.A. 2004. Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. Mol Cell 15:767-776.
134. Hebert, D.N., Zhang, J.X., Chen, W., Foellmer, B., and Helenius, A. 1997. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J Cell Biol 139:613-623.
135. Hegde, R.S., Mastrianni, J.A., Scott, M.R., Defea, K.A., Tremblay, P., Torchla, M., Dearmond, S.J., Prusiner, S.B., and Lingappa, V.R. 1998. A transmembrane form of the prion protein in neurodegenerative disease. Science 279:827-834.
136. Heinrich, S.U., Mothes, W., Brunner, J., and Rapoport, TA. 2000. The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain. Cell 102:233-244.
137. Heinrich, S.U. and Rapoport, T.A. 2003. Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane. Embo J 22:3654-3663.
138. Helenius, A. and Aebi, M. 2001. Intracellular functions of N-linked glycans. Science 291:2364-2369.
139. Helenius, A. and Aebi, M. 2004. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73:1019-1049.
140. Helenius, A., Marquardt, T., and Braakman, I. 1992. The endoplasmic reticulum as a protein-folding compartment. Trends Cell Biol 2:227-231.
141. Helenius, J. and Aebi, M. 2002. Transmembrane movement of dolichol linked carbohydrates during N-glycoprotein biosynthesis in the endoplasmic reticulum. Semin Cell Dev Biol 13:171-178.
142. Helm, K.W., Lafayette, P.R., Nagao, R.T., Key, J.L., and Vierling, E. 1993. Localization of small heat shock proteins to the higher plant endomembrane system. Mol Cell Biol 13:238-247.
143. Hendershot, L.M. 2004. The ER function BiP is a master regulator of ER function. Mt Sinai J Med 71:289-297.
144. Hendershot, L.M. and Bulleid, N.J. 2000. Protein-specific chaperones: the role of hsp47 begins to gel. Curr Biol 10:R912-R915.
145. Higy, M., Junne, T., and Spiess, M. 2004. Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 43:12716-12722.
146. Miller, M.M., Finger, A., Schweiger, M., and Wolf, D.H. 1996. ER degradation of a misfolded luminal protein by the cytosolic ubiqultin-proteasome pathway. Science 273:1725-1728.
147. Hirsch, C., Blom, D., and Ploegh, H.L. 2003. A role for N-glycanase in the cytosolic turnover of glycoproteins. Embo J 22:1036-1046.
148. Hobbs, H.H., Brown, M.S., and Goldstein, J.L. 1992. Molecular genetics of the LDL receptor gene in familial hypercholesterolemia. Hum Mutat 1:445-466.
149. Holmgren, A. 1985. Thioredoxin. Annu Rev Biochem 54:237-271.
150. Honoré, B. and Vorum, H. 2000. The CREC family, a novel family of multiple EF-hand, low-affinity Ca(2+)-binding proteins localised to the secretory pathway of mammalian cells. FEBS Lett 466:11-18.
151. Hoober, K.L., Glynn, N.M., Burnside, J., Coppock, D.L., and Thorpe, C. 1999a. Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxldases. J Biol Chem 274:31759-31762.
152. Hoober, K.L., Joneja, B., White, H.B., 3rd and Thorpe, C. 1996. A sulfhydryl oxidase from chicken egg white. J Biol Chem 271:30510-30516.
153. Hoober, K.L., Sheasley, S.L., Gilbert, H.F., and Thorpe, C. 1999b. Sulfhydryl oxidase from egg white. A facile catalyst for disulfide bond formation in proteins and peptides J Biol Chem 274:22147-22150.
154. Horibe, T., Gomi, M., Iguchi, D., Ito, H., Kitamura, Y., Masuoka, T., Tsujimoto, I., Kimura, T., and Kikuchi, M. 2004. Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to lsomerase activity and oxidative refolding. J Biol Chem 279:4604-4611.
155. Hosoda, A., Kimata, Y., Tsuru, A., and Kohno, K. 2003. JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs. J Biol Chem 278:2669-2676.
156. Hosokawa, N., Wada, I., Hasegawa, K., Yorihuzi, T., Tremblay, L.O., Herscovics, A., and Nagata, K. 2001. A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation. EMBO Rep 2:415-422.
157. Houry, W.A., Frishman, D., Eckerskorn, C., Lottspeich, F., and Hartl, F.D. 1999. Identification of in vivo substrates of the chaperonin GroEL. Nature 402:147-1 54.
158. Hseu, M.J., Yen, C.H., and Tzeng, M.C. 1999. Crocalbin: a new calcium-binding protein that is also a binding protein for crotoxin, a neurotoxic phospholipase A2. FEBS Lett 445:440-444.
159. Hsieh, J.C., Lee, L., Zhang, L., Wefer, S., Brown, K., Derossi, C., Wines, M.E., Rosenquist, T., and Holdener, B.C. 2003. Mesd encodes an LRP5/6 chaperone essential for specification of mouse embryonic polarity. Cell 112:355-367.
160. Huber-Wunderlich, M. and Glockshuber, R. 1998. A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold Des 3:161-171.
161. Huppa, J.B. and Ploegh, H.L. 1998. The eS-Sence of -SH in the ER. Cell 92:145-148.
162. Hurtley, S.M., Bole, D.G., Hoover-Litty, H., Helenius, A., and Copeland, C.S. 1989. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J Cell Biol 108:2117-2126.
163. Huyer, G., Longsworth, G.L., Mason, D.L., Mallampalli, M.P., Mccaffery, J.M., Wright, R.L., and Michaelis, S. 2004a. A striking quality control subcompartment in Saccharomyces cerevisiae: the endoplasmic reticulum-associated compartment. Mol Biol Cell 15:908-921.
164. Huyer, G., Piluek, W.F., Fansler, Z., Kreft, S.G., Hochstrasser, M., Brodsky, J.L., and Michaelis, S. 2004b. Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 279:38369-38378.
165. Hwang, C., Sinskey, A.J., and Lodish, H.F. 1992. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257:1496-1502.
166. Ikawa, M., Nakanishi, T., Yamada, S., Wada, I., Kominami, K., Tanaka, H., Nozaki, M., Nishimune, Y., and Okabe, M. 2001. Calmegin is required forfertilin alpha/beta heterodimerization and sperm fertility. Dev Biol 240:254-261.
167. Ikawa, M., Wada, I., Kominami, K., Watanabe, D., Toshimori, K., Nishimune, Y., and Okabe, M. 1997. The putative chaperone calmegin is required for sperm fertility. Nature 387:607-611.
168. Jaenicke, R. 1991. Protein folding: local structures, domains, subunits, and assemblies. Biochemistry 30:3147-3161.
169. Jakob, C.A., Bodmer, D., Spirig, U., Battig, P., Marcil, A., Dignard, D., Bergeron, J.J., Thomas, D.Y., and Aebi, M. 2001. Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast. EMBO Rep 2:423-430.
170. Jakob, C.A., Burda, P., Roth, J., and Aebi, M. 1998. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142:1223-1233.
171. Janolino, V.G. and Swaisgood, H.E. 1975. Isolation and characterization of sulfhydryl oxidase from bovine milk. J Biol Chem 250:2532-2538.
172. Jansens, A., Van Duijn, E., and Braakman, I. 2002. Coordinated nonvectorial folding in a newly synthesized multidomain protein. Science 298:2401-2403.
173. Jarosch, E., Taxis, C., Volkwein, C., Bordallo, J., Finley, D., Wolf, D.H., and Sommer, T. 2002. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4:134-139.
174. Jenni, S. and Ban, N. 2003. The chemistry of protein synthesis and voyage through the ribosomal tunnel. Curr Opin Struct Biol 13:212-219.
175. Jessop, C.E. and Bulleld, N.J. 2004. Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells. J Biol Chem 279:55341-55347.
176. Johnson, A.E. and Van Waes, M.A. 1999. The translocon: a dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol 15:799-842.
177. Johnson, J.L., Beito, T.G., Krco, C.J., and Toft, D.O. 1994. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol Cell Biol 14:1956-1963.
178. Kabani, M., Beckerich, J.M., and Gaillardin, C. 2000. SIs1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. Mol Cell Biol 20:6923-6934.
179. Kadokura, H., Tian, H., Zander, T., Bardwell, J.C., and Beckwith, J. 2004. Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science 303:534-537.
180. Kamhi-Nesher, S., Shenkman, M., Tolchinsky, S., Fromm, S.V., Ehrlich, R., and Lederkremer, G.Z. 2001. A novel quality control compartment derived from the endoplasmic reticulum. Mol Biol Cell 12:1711-1723.
181. Kaneko, M. and Nomura, Y. 2003. ER signaling in unfolded protein response. Life Sci 74:199-205.
182. Katiyar, S., Li, G., and Lennarz, W.J. 2004. A complex between peptide:
183. Keenan, R.J., Freymann, D.M., Stroud, R.M., and Walter, P. 2001. The signal recognition particle. Annu Rev Biochem 70:755-775.
184. Kellokumpu, S., Suokas, M., Risteli, L., and Myllyla, R. 1997. Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum. J Biol Chem 272:2770-2777.
185. Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M., and Creighton, T.E. 1997. The folding catalyst protein disulfide isomerase is constructed of active and inactivethioredoxin modules. Curr Biol 7:239-245.
186. Kemmink, J., Dijkstra, K., Mariani, M., Scheek, R.M., Penka, E., Nilges, M., and Darby, NJ. 1999. The structure in solution of the b domain of protein disulfide isomerase. J Biomol NMR 13:357-368.
187. Kerem, A., Kronman, C., Bar-Nun, S., Shafferman, A., and Velan, B. 1993. Interrelations between assembly and secretion of recombinant human acetylcholinesterase. J Biol Chem 268:180-184.
188. Kikkert, M., Doolman, R., Dai, M., Avner, R., Hassink, G., Van Voorden, S., Thanedar, S., Roitelman, J., Chau, V., and Wiertz, E. 2004. Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. J Biol Chem 279:3525-3534.
189. Kim, J.H., Johannes, L., Goud, B., Antony, C., Lingwood, C.A., Daneman, R., and Grinstein, S. 1998. Noninvasive measurement of the pH of the endoplasmic reticulum at rest and during calcium release. Proc Natl Acad Sci U S A 95:2997-3002.
190. Kim, P.K., Janiak-Spens, F., Trimble, W.S., Leber, B., and Andrews, D.W. 1997. Evidence for multiple mechanisms for membrane binding and integration via carboxyl-terminal insertion sequences. Biochemistry 36:8873-8882.
191. Kim, P.S. and Arvan, P. 1995. Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J Cell Biol 128:29-38.
192. Kim, P.S., Kim, K.R., and Arvan, P. 1993. Disulfide-linked aggregation of thyroglobulin normally occurs during nascent protein folding. Am J Physiol 265:C704-C711.
193. Klappa, P., Ruddock, L.W., Darby, N.J., and Freedman, R.B. 1998. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. Embo J 17:927-935.
194. Klausner, R.D., and Sitia, R. 1990. Protein degradation in the endoplasmic reticulum. Cell 62:611-614.
195. Knoblach, B., Keller, B.O., Groenendyk, J., Aldred, S., Zheng, J., Lemire, B.D., Li, L., and Michalak, M. 2003. ERp19 and ERp46, New Members of the Thioredoxin Family of Endoplasmic Reticulum Proteins. Mol Cell Proteomics 2:1104-1119.
196. Knop, M., Finger, A., Braun, T., Hellmuth, K., and Wolf, D.H. 1996. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. Embo J 15:753-763.
197. Koch, G., Smith, M., Macer, D., Webster, P., and Mortara, R. 1986. Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin. J Cell Sci 86:217-232.
198. Koch, G.L. 1990. The endoplasmic reticulum and calcium storage. Bioessays 12:527-531.
199. Kopito, R.R. 1997. ER quality control: the cytoplasmic connection. Cell 88:427-430.
200. Kopito, R.R. 1999. Biosynthesis and degradation of CFTR. Physiol Rev 79:5167-5173.
201. Kopito, R.R. and Sitia, R. 2000. Aggresomes and Russell bodies. Symptoms of cellular indigestion? EMBO Rep 1:225-231.
202. Kornfeld, R. and Kornfeld, S. 1985. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54:631-664.
203. Kostova, Z. and Wolf, D.H. 2003. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. Embo J 22:2309-2317.
204. Kowarik, M., Kung, S., Martoglio, B., and Helenius, A. 2002. Protein folding during cotranslational translocation in the endoplasmic reticulum. Mol Cell 10:769-778.
205. Kutay, U., Ahnert-Hilger, G., Hartmann, E., Wiedenmann, B., and Rapoport, TA. 1995. Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. Embo J 14:217-223.
206. Kuznetsov, G., Chen, L.B., and Nigam, S.K. 1994. Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation. J Biol Chem 269:22990-22995.
207. Lamantia, M.L. and Lennarz, W.J. 1993. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74:899-908.
208. Land, A., Zonneveld, D., and Braakman, I. 2003. Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage. Faseb 717:1058-1067.
209. Lander, E.S., Linton, L.M., Birren, B., Nusbaum, C., Zody, M.C., Baldwin, J., Devon, K., Dewar, K., Doyle, M., Fitzhugh, W., et al. 2001. Initial sequencing and analysis of the human genome. Nature 409:860-921.
210. Leavitt, R., Schlesinger, S., and Kornfeld, S. 1977. Tunicamycin inhibits glycosylation and multiplication of Sindbis and vesicular stomatitis viruses. J Virol 21:375-385.
211. Lehle, L. and Tanner, W. 1976. The specific site of tunicamycin inhibition in the formation of dolichol-bound N-acetylglucosamine derivatives. FEBS Lett 72:167-170.
212. Lehmann, S. and Harris, D.A. 1995. A mutant prion protein displays an aberrant membrane association when expressed in cultured cells. J Biol Chem 270:24589-24597.
213. Leitzgen, K., Knittler, M.R., and Haas, I.G. 1997. Assembly of immunoglobulin light chains as a prerequisite for secretion. A model for oligomerization-dependent subunit folding. J Biol Chem 272:3117-3123.
214. Letourneur, F., Gaynor, E.G., Hennecke, S., Demolliere, C., Duden, R., Emr, S.D., Riezman, H., and Cosson, P. 1994. Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Cell 79:1199-1207.
215. Li, Y., Bergeron, J.J., Luo, L., Ou, W.J., Thomas, D.Y., and Kang, C.Y. 1996. Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport. Proc Natl Acad Sci U S A 93:9606-9611.
216. Li, Y., Luo, L., Thomas, D.Y., and Kang, C.Y. 1994. Control of expression, glycosylation, and secretion of HIV-1 gp120 by homologous and heterologous signal sequences. Virology 204:266-278.
217. Liepinsh, E., Baryshev, M., Sharipo, A., Ingelman-Sundberg, M., Otting, G., and Mkrtchian, S. 2001. Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer. Structure (Camb) 9:457-471.
218. Lilley, B.N. and Ploegh, H.L. 2004. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429:834-840.
219. Lin, H.Y., Masso-Welch, P., Di, Y.P., Cai, J.W., Shen, J.W., and Subjeck, J.R. 1993. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Mol Biol Cell 4:1109-1119.
220. Lodish, H.F. and Kong, N. 1990. Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J Biol Chem 265:10893-10899.
221. Lodish, H.F. and Kong, N. 1991. Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum. J Biol Chem 266:14835-14838.
222. Lotz, G.P., Lin, H., Harst, A., and Obermann, W.M. 2003. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem 278:17228-17235.
223. Lukacs, G.L., Mohamed, A., Kartner, N., Chang, X.B., Riordan, J.R., and Grinstein, S. 1994. Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP. Embo J 13:6076-6086.
224. Lundstrom, J. and Holmgren, A. 1993. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry 32:6649-6655.
225. Ma, J. and Lindquist, S. 2002. Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 298:1785-1788.
226. Ma, J., Wollmann, R., and Lindquist, S. 2002. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298:1781-1785.
227. Macer, D.R. and Koch, G.L. 1988. Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum. J Cell Sci 91:61-70.
228. Mancini, R., Aebi, M., and Helenius, A. 2003. Multiple endoplasmic reticulum-associated pathways degrade mutant yeast carboxypeptidase Y in mammalian cells. J Biol Chem 278:46895-46905.
229. Margolese, L., Waneck, G.L., Suzuki, C.K., Degen, E., Flavell, R.A., and Williams, D.B. 1993. Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90). J Biol Chem 268:17959-17966.
230. Marshall, R.D. 1972. Glycoproteins. Annu Rev Biochem 41:673-702.
231. Martin, J.L., Bardwell, J.C., and Kuriyan, J. 1993. Crystal structure of the DsbA protein required for dtsulphide bond formation in vivo. Nature 365:464-468.
232. Martoglio, B. and Dobberstein, B. 1998. Signal sequences: more than just greasy peptides. Trends Cell Biol 8:410-415.
233. Martoglio, B., Hofmann, M.W., Brunner, J., and Dobberstein, B. 1995. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 81:207-214.
234. Mast, S.W., Diekman, K., Karaveg, K., Davis, A., Sifers, R.N., and Moremen, K.W. 2005. Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins. Glycobiology 15:421-436.
235. Matlack, K.E., Misselwitz, B., Plath, K., and Rapoport, T.A. 1999. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97:553-564.
236. Matlack, K.E. and Walter, P. 1995. The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane. J Biol Chem 270:6170-6180.
237. Matsuo, Y., Akiyama, N., Nakamura, H., Yodoi, J., Noda, M., and Kizaka-Kondoh, S. 2001. Identification of a novel thioredoxin-related transmembrane protein. J Biol Chem 276:10032-10038.
238. Matsuo, Y., Nishinaka, Y, Suzuki, S., Kojima, M., Kizaka-Kondoh, S., Kondo, N., Son, A., Sakakura-Nishiyama, J., Yamaguchi, Y., Masutani, H., et al. 2004. TMX, a human transmembrane oxidoreductase of the thioredoxin family: the possible role in disulfide-linked protein folding in the endoplasmic reticulum. Arch Biochem Biophys 423:81-87.
239. Mayer, M.P., Nikolay, R., and Bukau, B. 2002. Aha, another regulator for hsp90 chaperones. Mol Cell 10:1255-1256.
240. Mazzarella, R.A., Srinivasan, M., Haugejorden, S.M., and Green, M. 1990. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J Biol Chem 265:1094-1101.
241. Mcginnes, L.W. and Morrison, T.G. 1998. Role of carbohydrate processing and calnexin binding in the folding and activity of the HN protein of Newcastle disease virus. Virus Res 53:175-185.
242. Meacock, S.L., Lecomte, F.J., Crawshaw, S.G., and High, S. 2002. Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein. Mol Biol Cell 13:4114-4129.
243. Medeiros-Neto, G., Kim, P.S., Yoo, S.E., Vono, J., Targovnik, H.M., Camargo, R., Hossain, S.A., and Arvan, P. 1996. Congenital hypothyroid goiter with deficient thyroglobulin. Identification of an endoplasmic reticulum storage disease with induction of molecular chaperones. J Clin Invest 98:2838-2844.
244. Medicherla, B., Kostova, Z., Schaefer, A., and Wolf, D.H. 2004. Agenomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Rep 5:692-697.
245. Mehta, A., Zitzmann, N., Rudd, P.M., Block, T.M., and Dwek, R.A. 1998. Alpha-glucosidase inhibitors as potential broad based anti-viral agents. FEBS Lett 430:17-22.
246. Meldolesi, J. and Pozzan, T. 1998. The endoplasmic reticulum Ca2+ store: a view from the lumen. Trends Biochem Sci 23:10-14.
247. Melnick, J., Aviel, S., and Argon, Y. 1992. The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J Biol Chem 267:21303-21306.
248. Melnick, J., Dul, J.L., and Argon, Y. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370:373-375.
249. Meng, X., Zhang, C., Chen, J., Peng, S., Cao, Y., Ying, K., Xie, Y., and Mao, Y. 2003. Cloning and identification of a novel cDNA coding thioredoxin-related transmembrane protein 2. Biochem Genet 41:99-106.
250. Mesaeli, N., Nakamura, K., Zvaritch, E., Dickie, P., Dziak, E., Krause, K.H., Opas, M., Maclennan, D.H., and Michalak, M. 1999. Calreticulin is essential for cardiac development. J Cell Biol 144:857-868.
251. Meunier, L., Usherwood, Y.K., Chung, K.T., and Hendershot, L.M. 2002. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13:4456-4469.
252. Mezghrani, A., Fassio, A., Benham, A., Simmen, I, Braakman, I., and Sitia, R. 2001. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. Embo J 20:6288-6296.
253. Miller, E., Antonny, B., Hamamoto, S., and Schekman, R. 2002. Cargo selection into COPII vesicles is driven by the Sec24p subunit. Embo J 21:6105-6113.
254. Miller, E.A., Beilharz, T.H., Malkus, P.N., Lee, M.C., Hamamoto, S., Orci, L., and Schekman, R. 2003. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114:497-509.
255. Miller, J.D., Wilhelm, H., Gierasch, L., Gilmore, R., and Walter, P. 1993. GTP binding and hydrolysis by the signal recognition particle during nitiation of protein translocation. Nature 366:351-354.
256. Milstein, C. 1965. Interchain disulphide bridges in Bence-Jones proteins and in gamma-globulins B chains. Nature 205:1171-1173.
257. Mingarro, I., Nilsson, I., Whitley, P., and Von Heijne, G. 2000. Different conformations of nascent polypeptides during translocation across the ER membrane. BMC Cell Biol 1:3.
258. Misselwitz, B., Staeck, O., Matlack, K.E., and Rapoport, T.A. 1999. Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex. J Biol Chem 274:20110-20115.
259. Misselwitz, B., Staeck, O., and Rapoport, T.A. 1998. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol Cell 2:593-603.
260. Mkrtchian, S., Fang, C., Hellman, U., and Ingelman-Sundberg, M. 1998. A stress-inducible rat liver endoplasmic reticulum protein, ERp29. Eur J Biochem 2 51:304-313.
261. Moise, A.R., Grant, J.R., Lippe, R., Gabathuler, R., and Jefferies, W.A. 2004. The adenovirus E3-6.7K protein adopts diverse membrane topologies following posttranslational translocation. J Virol 78:454-463.
262. Molinari, M., Calanca, V., Galli, C., Lucca, P., and Paganetti, P. 2003. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299:1397-1400.
263. Molinari, M., Eriksson, K.K., Calanca, V., Galli, C., Cresswell, P., Michalak, M., and Helenius, A. 2004. Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol Cell 13:125-135.
264. Molinari, M., Galli, C., Piccaluga, V., Pieren, M., and Paganetti, P. 2002. Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. J Cell Biol 158:247-257.
265. Molinari, M. and Helenius, A. 1999. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402:90-93.
266. Molinari, M. and Helenius, A. 2000. Chaperone selection during glycoprotein translocation nto the endoplasmic reticulum. Science 288:331-333.
267. Molteni, S.N., Fassio, A., Ciriolo, M.R., Filomeni, G., Pasqualetto, E., Fagioli, C., and Sitia, R. 2004. Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum. J Biol Chem 279:32667-32673.
268. Morello, J.P., Salahpour, A., Laperriere, A., Bernier, V., Arthus, M.F., Lonergan, M., Petaja-Repo, U., Angers, S., Morin, D., Bichet, D.G., et al. 2000. Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants. J Clin Invest 105:887-895.
269. Mossessova, E., Bickford, L.C., and Goldberg, J. 2003. SNARE selectivity of the COPII coat. Cell 114:483-495.
270. Mothes, W., Heinrich, S.U., Graf, R., Nilsson, I., Von Heijne, G., Brunner, J., and Rapoport, T.A. 1997. Molecular mechanism of membrane protein integration into the endoplasmic reticulum. Cell 89:523-533.
271. Muniz, M., Morsomme, P., and Riezman, H. 2001. Protein sorting upon exit from the endoplasmic reticulum. Cell 104:313-320.
272. Muniz, M., Nuoffer, C., Hauri, H.P., and Riezman, H. 2000. The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles. J Cell Biol 148:925-930.
273. Munro, S. and Pelham, H.R. 1987. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48:899-907.
274. Nagai, N., Hosokawa, M., Itohara, S., Adachi, E., Matsushita, T., Hosokawa, N., and Nagata, K. 2000. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J Cell Biol 150:1499-1506.
275. Nagata, K., Saga, S., and Yamada, K.M. 1988. Characterization of a novel transformation-sensitive heat-shock protein (HSP47) that binds to collagen. Biochem Biophys Res Commun 153:428-434.
276. Nakamura, T., Yabe, D., Kanazawa, N., Tashiro, K., Sasayama, S., and Honjo, T. 1998. Molecular cloning, characterization, and chromosomal localization of FKBP23, a novel FK506-binding protein with Ca2+-binding ability. Genomics 54:89-98.
277. Nakatsukasa, K., Nishikawa, S., Hosokawa, N., Nagata, K., and Endo, T. 2001. Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins. J Biol Chem 276:8635-8638.
278. Nicola, A.V., Chen, W., and Helenius, A. 1999. Co-translational folding of an alphavirus capsid protein in the cytosol of living cells. Nat Cell Biol 1:341-345.
279. Nieland, T.J., Tan, M.C., Monne-Van Muijen, M., Koning, F., Kruisbeek, A.M., and Van Bleek, G.M. 1996. Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein GP96/GRP94. Proc Natl Acad Sci U S A 93:6135-6139.
280. Nigam, S.K., Goldberg, A.L., Ho, S., Rohde, M.F., Bush, K.T., and Sherman, M. 1994. A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily. J Biol Chem 269:1744-1749.
281. Nigam, S.K., Jin, Y.J., Jin, M.J., Bush, K.T., Bierer, B.E., and Burakoff, S.J. 1993. Localization of the FK506-binding protein, FKBP 13, to the lumen of the endoplasmic reticulum. Biochem J 294:511-515.
282. Nilsson, I., Witt, S., Kiefer, H., Mingarro, I., and Von Heijne, G. 2000. Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane. J Biol Chem 275:6207-6213.
283. Nilsson, I.M. and Von Heijne, G. 1993. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J Biol Chem 268:5798-5801.
284. Nilsson, T., Jackson, M., and Peterson, P.A. 1989. Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell 58:707-718.
285. Nishikawa, S. and Endo, T. 1997. The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion. J Biol Chem 272:12889-12892.
286. Nishikawa, S.I., Fewell, S.W., Kato, Y., Brodsky, J.L., and Endo, T. 2001. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 153:1061-1070.
287. Nishimura, N. and Balch, W.E. 1997. A di-acidic signal required for selective export from the endoplasmic reticulum. Science 277:556-558.
288. Nørgaard, P., Westphal, V., Tachibana, C., Alsoe, L., Holst, B., and Winther, J.R. 2001. Functional differences in yeast protein disulfide isomerases. J Cell Biol 152:553-562.
289. Nørgaard, P. and Winther, J. R. 2001. Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity. Biochem J 358:269-274.
290. Oda, Y., Hosokawa, N., Wada, I., and Nagata, K. 2003. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299:1394-1397.
291. Olivari, S., Galli, C., Alanen, H., Ruddock, L., and Molinari, M. 2004. A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation. J Biol Chem.
292. Oliver, J.D., Roderick, H.L., Llewellyn, D.H., and High, S. 1999. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol Biol Cell 10:2573-2582.
293. Oliver, J.D., Van Der Wal, F.J., Bulleid, N.J., and High, S. 1997. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275:86-88.
294. Østergaard, H., Tachibana, C., and Winther, J.R. 2004. Monitoring disulfide bond formation in the eukaryotic cytosol. J Cell Biol 166:337-345.
295. Otte, S. and Barlowe, C. 2004. Sorting signals can direct receptor-mediated export of soluble proteins into COPII vesicles. Nat Cell Biol 6:1189-1194.
296. Otteken, A., Earl, P.L., and Moss, B. 1996. Folding, assembly, and intracellular trafficking of the human immunodeficiency virus type 1 envelope glycoprotein analyzed with monoclonal antibodies recognizing maturational intermediates. J Virol 70:3407-3415.
297. Ou, W.J., Cameron, P.H., Thomas, D.Y., and Bergeron, J.J. 1993. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364:771-776.
298. Ozawa, M. and Muramatsu, T. 1993. Reticulocalbin, a novel endoplasmic reticulum resident Ca(2+)-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence. J Biol Chem 268:699-705.
299. Pagani, M., Fabbri, M., Benedetti, C., Fassio, A., Pilati, S., Bulleid, N.J., Cabibbo, A., and Sitia, R. 2000. Endoplasmic reticulum oxidoreductin 1-Ibeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem 275:23685-23692.
300. Palade, G. 1975. Intracellular aspects of the process of protein synthesis. Science 189:347-358.
301. Panaretou, B., Siligardi, G., Meyer, P., Maloney, A., Sullivan, J.K., Singh, S., Millson, S.H., Clarke, P.A., Naaby-Hansen, S., Stein, R., et al. 2002. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell 10:1307-1318.
302. Park, J., Easton, D.P., Chen, X., Macdonald, I.J., Wang, X.Y., and Subjeck, J.R. 2003. The chaperoning properties of mouse grp170, a member of the third family of hsp70 related proteins. Biochemistry 42:14893-14902.
303. Parlati, F., Dominguez, M., Bergeron, J.J., and Thomas, D.Y. 1995. Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J Biol Chem 270:244-253.
304. Parodi, A.J. 1999. Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells. Biochim Biophys Acta 1426:287-295.
305. Parodi, A.J. 2000. Protein glucosylation and its role in protein folding. Annu Rev Biochem 69:69-93.
306. Patil, C. and Walter, P. 2001. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 13:349-355.
307. Patterson, C.E., Schaub, T, Coleman, E.J., and Davis, E.G. 2000. Developmental regulation of FKBP65. An ER-localized extracellular matrix binding-protein. Mol Biol Cell 11:3925-3935.
308. Pelham, H.R. 1990. The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem Sci 15:483-486.
309. Perlmutter, D.H. 1996. Alpha-1-antitrypsin deficiency: biochemistry and clinical manifestations. Ann Med 28:385-394.
310. Persson, S., Rosenquist, M., and Sommarin, M. 2002. Identification of a novel calreticulin isoform (Crt2) in human and mouse. Gene 297:151-158.
311. Peterson, J.R. and Helenius, A. 1999. In vitro reconstitution of calreticulin-substrate interactions. J Cell Sci 112:2775-2784.
312. Peterson, J.R., Ora, A., Van, P.N., and Helenius, A. 1995. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol Biol Cell 6:1173-1184.
313. Pilon, M., Schekman, R., and Romisch, K. 1997. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. Embo J 16:4540-4548.
314. Pirneskoski, A., Klappa, P., Lobell, M., Williamson, R.A., Byrne, L., Alanen, H.I., Salo, K.E., Kivirikko, K.I., Freedman, R.B., and Ruddock, L.W. 2004. Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. J Biol Chem 279:10374-10381.
315. Plemper, R.K., Bohmler, S., Bordallo, J., Sommer, T., and Wolf, D.H. 1997. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388:891-895.
316. Pollard, M.G., Travers, K.J., and Weissman, J.S. 1998. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1:171-182.
317. Price, E.R., Zydowsky, L.D., Jin, M.J., Baker, C.H., Mckeon, F.D., and Walsh, C.T. 1991. Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. Proc Natl Acad Sci U S A 88:1903-1907.
318. Raje, S. and Thorpe, C. 2003. Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: role of a thioredoxin domain in disulfide bond formation. Biochemistry 42:4560-4568.
319. Rane, N.S., Yonkovich, J.L., and Hegde, R.S. 2004. Protection from cytosolic prion protein toxicity by modulation of protein translocation. Embo J 23:4550-4559.
320. Rao, H. and Sastry, A. 2002. Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277: 11691-11695.
321. Rapoport, T.A., Matlack, K.E., Plath, K., Misselwitz, B., and Staeck, O. 1999. Posttranslational protein translocation across the membrane of the endoplasmic reticulum. Biol Chem 380:1143-1150.
322. Reddy, P., Sparvoli, A., Fagioli, C., Fassina, G., and Sitia, R. 1996. Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains. Embo J 15:2077-2085.
323. Reddy, P.S. and Corley, R.B. 1998. Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum. Bioessays 20:546-554.
324. Ritter, C. and Helenius, A. 2000. Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase. Nat Struct Biol 7:278-280.
325. Rossanese, O.W., Soderholm, J., Bevis, B.J., Sears, I.B., O'connor, J., Williamson, E.K., and Glick, B.S. 1999. Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J Cell Biol 145:69-81.
326. Rosser, M.F., and Nicchitta, C.V. 2000. Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. I. Evidence for allosteric regulation of ligand binding. J Biol Chem 275:22798-22805.
327. Rosser, M.F., Trotta, B.M., Marshall, M.R., Berwin, B., and Nicchitta, C.V. 2004. Adenosine nucleotides and the regulation of GRP94-client protein interactions. Biochemistry 43:8835-8845.
328. Rudd, P.M. and Dwek, R.A. 1997. Glycosylation: heterogeneity and the 3D structure of proteins. Crit Rev Biochem Mol Biol 32:1-100.
329. Russell, S.J., Ruddock, L.W., Salo, K.E., Oliver, J.D., Roebuck, Q.P., Llewellyn, D.H., Roderick, H.L., Koivunen, P., Myllyharju, J., and High, S. 2004. The Primary Substrate Binding Site in the b′ Domain of ERp57 Is Adapted for Endoplasmic Reticulum Lectin Association. J Biol Chem 279:18861-18869.
330. Rutishauser, J. and Spiess, M. 2002. Endoplasmic reticulum storage diseases. Swiss Med Wkly 132:211-222.
331. Sadasivan, B., Lehner, P.J., Ortmann, B., Spies, T., and Cresswell, P. 1996. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5:103-114.
332. Sanders, S.L., Whitfield, K.M., Vogel, J.P., Rose, M.D., and Schekman, R.W. 1992. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell 69:353-365.
333. Saris, N., Holkeri, H., Craven, R.A., Stirling, C.J., and Makarow, M. 1997. The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates. J Cell Biol 137:813-824.
334. Saris, N. and Makarow, M. 1998. Transient ER retention as stress response: conformational repair of heat-damaged proteins to secretion-competent structures. J Cell Sci 111:1575-1582.
335. Sato, Y., Sakaguchi, M., Goshima, S., Nakamura, T., and Uozumi, N. 2003. Molecular dissection of the contribution of negatively and positively charged residues in S2, S3, and S4 to the final membrane topology of the voltage sensor in the K+ channel, KAT1. J Biol Chem 278:13227-13234.
336. Schaiff, W.T., Hruska, K.A., Jr., Mccourt, D.W., Green, M., and Schwartz, B.D. 1992. HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J Exp Med 176:657-666.
337. Scheel, A.A. and Pelham, H.R. 1996. Purification and characterization of the human KDEL receptor. Biochemistry 35:10203-10209.
338. Scherer, P.E., Lederkremer, G.Z.,Williams, S., Fogliano, M., Baldini, G., and Lodish, H.F. 1996. Cab45, a novel (Ca2+)-binding protein localized to the Golgi lumen. J Cell Biol 133:257-268.
339. Schlenstedt, G., Harris, S., Risse, B., Lill, R., and Silver, P.A. 1995. A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J Cell Biol 129:979-988.
340. Schmid, F.X., Mayr, L.M., Mucke, M., and Schonbrunner, E.R. 1993. Prolyl isomerases: role in protein folding. Adv Protein Chem 44:25-66.
341. Schrag, J.D., Bergeron, J.J., Li, Y., Borisova, S., Hahn, M., Thomas, D.Y., and Cygler, M. 2001. The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol Cell 8:633-644.
342. Schröder, M. and Kaufman, R.J. 2005. ER stress and the unfolded protein response. Mutat Res 569:29-63.
343. Schutze, M.P., Peterson, P.A., and Jackson, M.R. 1994. An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum. Embo J 13:1696-1705.
344. Schwaller, M., Wilkinson, B., and Gilbert, H.F. 2003. Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase. J Biol Chem 278:7154-7159.
345. Sevier, C.S., Cuozzo, J.W., Vala, A., Aslund, F., and Kaiser, C.A. 2001. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat Cell Biol 3:874-882.
346. Sevier, C.S. and Kaiser, C.A. 2002. Formation and transfer of disulphide bonds in living cells. Nat Rev Mol Cell Biol 3:836-847.
347. Shadidy, M., Caubit, X., Olsen, R., Seternes, O.M., Moens, U., and Krauss, S. 1999. Biochemical analysis of mouse FKBP60, a novel member of the FKPB family. Biochim Biophys Acta 1446:295-307.
348. Shaw, A.S., Rottier, P.J., and Rose, J.K. 1988. Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proc Natl Acad Sci U S A 85:7592-7596.
349. Shen, Y., Meunier, L., and Hendershot, L.M. 2002. Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress. J Biol Chem 277:15947-15956.
350. Sitia, R., Neuberger, M., Alberini, C., Bet, P., Fra, A., Valetti, C., Williams, G., and Milstein, C. 1990. Developmental regulation of IgM secretion: the role of the carboxy- terminal cysteine. Cell 60:781-790.
351. Skowronek, M.H., Rotter, M., and Haas, I.G. 1999. Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog. Biol Chem 380:1133-1138.
352. Smith, D.F., Stensgard, B.A., Welch, W.J., and Toft, D.O. 1992. Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events. J Biol Chem 267:1350-1356.
353. Soldano, K.L., Jivan, A., Nicchitta, C.V., and Gewirth, D.T. 2003. Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation. J Biol Chem 278:48330-48338.
354. Solovyov, A., Xiao, R., and Gilbert, H.F. 2004. Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae. J Biol Chem 279:34095-34100.
355. Sommer, T. and Jentsch, S. 1993. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365:176-179.
356. Song, J.L. and Wang, C.C. 1995. Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese. Eur J Biochem 231:312-316.
357. Sousa, M.C., Ferrero-Garcta, M.A., and Parodi, A.J. 1992. Recognition of the oiigosaccharide and protein moieties of glycoproteins by the UDP-Glcglycoprotein glucosyltransferase. Biochemistry 31:97-105.
358. Spee, P., Subjeck, J., and Neefjes, J. 1999. Identification of novel peptide binding proteins in the endoplasmic reticulum: ERp72, calnexin, and
359. Spooner, R.A., Watson, P.D., Marsden, C.J., Smith, D.C., Moore, K.A., Cook, J.P., Lord, J.M., and Roberts, L.M. 2004. Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum. Biochem J 383:285-293.
360. Steel, G.J., Fullerton, D.M., Tyson, J.R., and Stirling, C.J. 2004. Coordinated activation of Hsp70 chaperones. Science 303:98-101.
361. Steinmann, B., Bruckner, P., and Superti-Furga, A. 1991. Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase. J Biol Chem 266:1299-1303.
362. Stevens, F.J. and Argon, Y. 1999. Protein folding in the ER. Semin Cell Dev Biol 10:443-454.
363. Stewart, R.S., Drisaldi, B., and Harris, D.A. 2001. A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic Reticulum. Mol Biol Cell 12:881-889.
364. Stirling, C.J., Rothblatt, J., Hosobuchi, M., Deshaies, R., and Schekman, R. 1992. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol Biol Cell 3:129-142.
365. Sullivan, D.C., Huminiecki, L., Moore, J.W., Boyle, J.J., Poulsom, R., Creamer, D., Barker, J., and Bickneil, R. 2003. EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor. J Biol Chem 278:47079-47088.
366. Suzuki, T., Park, H., Kwofie, M.A., and Lennarz, W.J. 2001. Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast. J Biol Chem 276:21601-21607.
367. Swanson, R., Locher, M., and Hochstrasser, M. 2001. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 represser degradation. Genes Dev 15:2660-2674.
368. Swanton, E., High, S., and Woodman, P. 2003. Role of calnexin in the glycan-independent quality control of proteolipid protein. Embo J 22:2948-2958.
369. Tabak, H.F., Murk, J.L., Braakman, I., and Geuze, H.J. 2003. Peroxisomes start their life in the endoplasmic reticulum. Traffic 4:512-518.
370. Tachtbana, C. and Stevens, T.H. 1992. The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12:4601-4611.
371. Tachikawa, H., Funahashi, W., Takeuchi, Y., Nakanishi, H., Nishihara, R., Katoh, S., Gao, X.D., Mizunaga, T., and Fujimoto, D. 1997. Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner. Biochem Biophys Res Commun 239:710-714.
372. Tachikawa, H., Takeuchi, Y., Funahashi, W., Miura, T., Gao, X.D., Fujimoto, D., Mizunaga, T., and Onodera, K. 1995. Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett 369:212-216.
373. Tatu, U., Hammond, C., and Helenius, A. 1995. Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment. Embo J 14:1340-1348.
374. Tatu, U. and Helenius, A. 1997. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J Cell Biol 136:555-565.
375. Taxis, C., Hitt, R., Park, S.H., Deak, P.M., Kostova, Z., and Wolf, D.H. 2003. Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J Biol Chem 278:35903-35913.
376. Taxis, C., Vogel, F., and Wolf, D.H. 2002. ER-golgi traffic is a prerequisite for efficient ER degradation. Mol Biol Cell 13:1806-1818.
377. Taylor, S.C., Thibault, P., Tessier, D.C., Bergeron, J.J., and Thomas, D.Y. 2003. Glycopeptide specificity of the secretory protein folding sensor UDP-glucose glycoprotein:glucosyltransferase. EMBO Rep 4:405-411.
378. Teasdale, R.D., and Jackson, M.R. 1996. Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus. Annu Rev Cell Dev Biol 12:27-54.
379. Teckman, J.H., Burrows, J., Hidvegi, T., Schmidt, B., Hale, P.D., and Perimutter, D.H. 2001. The proteasome participates in degradation of mutant alpha 1-antitrypsin Z in the endoplasmic reticulum of hepatoma-derived hepatocytes. J Biol Chem 276:44865-44872.
380. Teckman, J.H. and Perlmutter, D.H. 2000. Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response. Am J Physiol Gastrointest Liver Physiol 279:G961-G974.
381. Thorpe, C., Hoober, K.L., Raje, S., Glynn, N.M., Burnside, J., Turi, G.K., and Coppock, D.L. 2002. Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Arch Biochem Biophys 405:1-12.
382. Tirosh, B., Furman, M.H., Tortorella, D., and Ploegh, H.L. 2003. Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocation. J Biol Chem 278:6664-6672.
383. Travers, K.J., Patil, C.K., Wodicka, L., Lockhart, D.J., Weissman, J.S., and Walter, P. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101:249-258.
384. Tremblay, L.O. and Herscovics, A. 1999. Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 Isomer B during N-glycan biosynthesis. Glycobiology 9:1073-1078.
385. Trombetta, E.S. and Helenius, A. 1998. Lectins as chaperones in glycoprotein folding. Curr Opin Struct Biol 8:587-592.
386. Trombetta, E.S. and Parodi, A.J. 2003. Quality control and protein folding in the secretory pathway. Annu Rev Cell Dev Biol 19:649-676.
387. Trombetta, S.E. and Parodi, A.J. 1992. Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase. J Biol Chem 267:9236-9240.
388. Tsai, B. and Rapoport, TA. 2002. Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1. J Cell Biol 159:207-216.
389. Tsai, B., Rodighiero, C., Lencer, W.I., and Rapoport, T.A. 2001. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104:937-948.
390. Tsai, B., Ye, Y., and Rapoport, T.A. 2002. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 3:246-255.
391. Tu, B.P., Ho-Schleyer, S.C., Travers, K.J., and Weissman, J.S. 2000. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290:1571-1574.
392. Tu, B.P and Weissman, J.S. 2002. The FAD- and O(2)-Dependent Reaction Cycle of Ero1-Mediated Oxidative Protein Folding in the Endoplasmic Reticulum. Mol Cell 10:983-994.
393. Tu, B.P. and Weissman, J.S. 2004. Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164:341-346.
394. Tyedmers, J., Lerner, M., Bies, C., Dudek, J., Skowronek, M.H., Haas, I.G., Helm, N., Nastainczyk, W., Volkmer, J., and Zimmermann, R. 2000. Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes. Proc Natl Acad Sci U S A 97:7214-7219.
395. Tyedmers, J., Lerner, M., Wiedmann, M., Volkmer, J., and Zimmermann, R. 2003. Polypeptide-binding proteins mediate completion of co-translational protein translocation into the mammalian endoplasmic reticulum. EMBO Rep 4:505-510.
396. Tyson, J.R. and Stirling, C.J. 2000. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. Embo J 19:6440-6452.
397. Udenfriend, S. and Kodukula, K. 1995. How glycosylphosphatidylinositol- anchored membrane proteins are made. Annu Rev Biochem 64:563-591.
398. Ditto, J. and Prockop, D.J. 1974. Intracellular hydroxylation of non-helical protocollagen to form triple-helical procollagen and subsequent secretion of the molecule. Eur J Biochem 43:221-230.
399. Ulloa-Aguirre, A., Janovick, J.A., Brothers, S.P., and Conn, P.M. 2004. Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease. Traffic 5:821-837.
400. Urade, R., Nasu, M., Moriyama, T., Wada, K., and Kito, M. 1992. Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum. J Biol Chem 267:15152-15159.
401. Van Anken, E., Romijn, E.P, Maggiont, C., Mezghrani, A., Sitia, R., Braakman, I., and Heck, A.J. 2003. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity 18:243-253.
402. Van Den Berg, B., Clemons, W.M., Jr., Collinson, I., Modis, Y., Hartmann, E., Harrison, S.C., and Rapoport, T.A. 2004. X-ray structure of a protein-conducting channel. Nature 427:36-44.
403. Van Leeuwen, J.E. and Kearse, K.P. 1996. Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes. Proc Natl Acad Sci U S A 93:13997-14001.
404. Van Lith, M., Hartigan, N., Hatch, J., and Benham, A.M. 2005. PDILT: A divergent testis-specific PDI with a non-classical SXXC motif that engages in disulfide dependent interactions in the endoplasmic reticulum. J Biol Chem 280:1376-1383.
405. Van Montfort, R., Slingsby, C., and Vierling, E. 2001. Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv Protein Chem 59:105-156.
406. Varga, K., Jurkuvenaite, A., Wakefield, J., Hong, J.S., Guimbellot, J.S., Venglarik, C.J., Niraj, A., Mazur, M., Sorscher, E.J., Collawn, J.F., et al. 2004. Efficient intracellular processing of the endogenous cystic fibrosis transmembrane conductance regulator in epithelial cell lines. J Biol Chem 279:22578-22584.
407. Vashist, S., Kim, W., Beiden, W.J., Spear, E.D., Barlowe, C., and Ng, D.T. 2001. Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding. J Cell Biol 155:355-368.
408. Vashist, S. and Ng, D.T. 2004. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J Cell Biol 165:41-52.
409. Volkmer, J., Guth, S., Nastainczyk, W., Knippel, P., Klappa, P., Gnau, V., and Zimmermann, R. 1997. Pancreas specific protein disulfide isomerase, PDIp, is in transient contact with secretory proteins during late stages of translocation. FEBS Lett 406:291-295.
410. Von Heijne, G. 1989. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341:456-458.
411. Von Heijne, G. and Gavel, Y. 1988. Topogenic signals in integral membrane proteins. Eur J Biochem 174:671-678.
412. Votsmeier, C. and Gallwitz, D. 2001. An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export. Embo J 20:6742-6750.
413. Vuori, K., Myllyla, R., Pihlajaniemi, T., and Kivirikko, K.I. 1992. Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity. J Biol Chem 267:7211-7214.
414. Walter, P. and Johnson, A.E. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol 10:87-119.
415. Wang, C.C. and Tsou, C.L. 1993. Protein disulfide isomerase is both an enzyme and a chaperone. Faseb J 7:1515-1517.
416. Wang, Q. and Chang, A. 1999. Eps1, a novel PDI-related protein involved in ER quality control in yeast. Embo J 18:5972-5982.
417. Wang, Q. and Chang, A. 2003. Substrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase family. Embo J 22:3792-3802.
418. Wang, S., Trumble, W.R., Liao, H., Wesson, C.R., Dunker, A.K., and Kang, C.H. 1998. Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. Nat Struct Biol 5:476-483.
419. Wang, X., Maltesen, J., An, Y., Moyer, B., Yoo, J.S., Bannykh, S., Wilson, I.A., Riordan, J.R., and Balch, W.E. 2004. COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code. J Cell Biol 167:65-74.
420. Ward, C.L. and Kopito, R.R. 1994. Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J Biol Chem 269:25710-25718.
421. Ward, C.L., Omura, S., and Kopito, R.R. 1995. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83:121-127.
422. Watanabe, D., Yamada, K., Nishina, Y., Tajima, Y., Koshimizu, U., Nagata, A., and Nishimune, Y. 1994. Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development. J Biol Chem 269:7744-7749.
423. Weis, K., Griffiths, G., and Lamond, A.I. 1994. The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif. J Biol Chem 269:19142-19150.
424. Weissman, J.S. and Kim PS. 1993. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365:185-188.
425. Werner, E.D., Brodsky, J.L., and Mccracken, A.A. 1996. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc Natl Acad Sci U S A 93:13797-13801.
426. Whitley, P., Grahn, E., Kutay, U., Rapoport, T.A., and Von Heijne, G. 1996. A 12-residue-long polyleucine tail is sufficient to anchor synaptobrevin to the endoplasmic reticulum membrane. J Biol Chem 271:7583-7586.
427. Wieland, F.T., Gleason, M.L., Serafini, T.A., and Rothman, J.E. 1987. The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell 50:289-300.
428. Wiertz, E.J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T.R., Rapoport, T.A., and Ploegh, H.L. 1996. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384:432-438.
429. Wilson, D.W., Lewis, M.J., and Pelham, H.R. 1993. pH-dependent binding of KDEL to its receptor in vitro. J Biol Chem 268:7465-7468.
430. Winkeler, A., Godderz, D., Herzog, V., and Schmitz, A. 2003. BiP-dependent export of cholera toxin from endoplasmic reticulum-derived microsomes. FEBS Lett 554:439-442.
431. Woolhead, C.A., Mccormick, P.J., and Johnson, A.E. 2004. Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 116:725-736.
432. Wrammert, J., Kallberg, E., and Leanderson, T. 2004. Identification of a novel thioredoxin-related protein, PC-TRP, which is preferentially expressed in plasma cells. Eur J Immunol 34:137-146.
433. Wunderlich, M. and Glockshuber, R. 1993. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci 2:717-726.
434. Xiao, R., Wilkinson, B., Solovyov, A., Winther, J.R., Holmgren, A., Lundstrom-Ljung, J., and Gilbert, H.F. 2004. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J Biol Chem 279:49780-49786.
435. Yabe, D., Nakamura, T., Kanazawa, N., Tashiro, K., and Honjo, T. 1997. Calumenin, a Ca2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEF. J Biol Chem 272:18232-18239.
436. Yamada, S., Ono, T., Mizuno, A., and Nemoto, T.K. 2003. A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone. Eur J Biochem 270:146-154.
437. Yao, Y., Zhou, Y., and Wang, C. 1997. Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2. Ernbo J 16:651-658.
438. Ye, Y., Meyer, H.H., and Rapoport, T.A. 2001. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414:652-656.
439. Ye, Y., Meyer, H.H., and Rapoport, T.A. 2003. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162:71-84.
440. Ye, Y., Shibata, Y., Yun, C., Ron, D., and Rapoport, T.A, 2004. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429:841-847.
441. Yoshida, Y., Chiba, T., Tokunaga, F., Kawasaki, H., Iwai, K., Suzuki, T., Ito, Y., Matsuoka, K., Yoshida, M., Tanaka, K. et al. 2002. E3 ubiquitin ligase that recognizes sugar chains. Nature 418:438-442.
442. Yoshida, Y., Tokunaga, F., Chiba, T., Iwai, K., Tanaka, K., and Tai, T. 2003. Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. J Biol Chem 278:43877-43884.
443. Young, J.C., Agashe, V.R., Siegers, K., and Hartl, F.U. 2004. Pathways of chaperone-mediated protein folding in the cytosol. Nat Rev Mol Cell Biol 5:781-791.
444. Yu, M., Haslam, R.H., and Haslam, D.B. 2000. HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells. J Biol Chem 275:24984-24992.
445. Zapun, A., Darby, N.J., Tessier, D.C., Michalak, M., Bergeron, J.J., and Thomas, D.Y. 1998. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J Biol Chem 273:6009-6012.
446. Zerangue, N., Schwappach, B., Jan, Y.N., and Jan, L.Y. 1999. A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. Neuron 22:537-548.
447. Zhang, J.X., Braakman, I., Matlack, K.E., and Helenius, A. 1997. Quality control in the secretory pathway: the role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations. Mol Biol Cell 8:1943-1954.
448. Zhong, X., Shen, Y., Ballar, P., Apostolou, A., Agami, R., and Fang, S. 2004. AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation. J Biol Chem 279:45676-45684.
449. Zimmermann, R. 1998. The role of molecular chaperones in protein transport into the mammalian endoplasmic reticulum. Biol Chem 379:275-282.
450. Zitzmann, N., Mehta, A.S., Carrouee, S., Butters, T.D., Platt, F.M., Mccauley, J., Blumberg, B.S., Dwek, R.A., and Block, T.M. 1999. Imino sugars inhibit the formation and secretion of bovine viral diarrhea virus, a pestivirus model of hepatitis C virus: implications for the development of broad spectrum anti-hepatitis virus agents. Proc Natl Acad Sci U S A 96:11878-11882.