Eukaryotic protein secretion

Current Opinion in Biotechnology

Volumn 8, Issue 5, 1997, Pages 595-601

  Sakaguchi, Masao ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE LINKED OLIGOSACCHARIDE; CALNEXIN; CHAPERONE; DOCKING PROTEIN; SECRETORY PROTEIN; SIGNAL PEPTIDE; SIGNAL RECOGNITION PARTICLE;

ENDOPLASMIC RETICULUM; EUKARYOTE; HUMAN; MEMBRANE TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN GLYCOSYLATION; PROTEIN SECRETION; PROTEIN SYNTHESIS; PROTEIN TARGETING; REVIEW;

EUKARYOTA;

EID: 0030660436     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(97)80035-3     Document Type: Article

References (77)

1. Schatz G, Dobberstein B: Common principles of protein translocation across membranes. Science 1996, 271:1519-1526. This review gives an extensive overview of the protein translocation process, including translocation across the ER, and translocation in E. coli, mitochondria, and chloroplast membranes.
2. Von Heijne G: The signal peptide. J Membr Biol 1990, 115:195-201.
3. Bird P, Gething M-J, Sambrook J: The functional efficiency of a mammalian signal peptide is directly related to its hydrophobicity. J Biol Chem 1990, 265:8420-8425.
4. Von Heijne G, Liljeström P, Mikus P, Andersson H, Ny T: The efficiency of the uncleaved secretion signal in the plasminogen activator inhibitor type 2 protein can be enhanced by point mutations that increase its hydrophobicity. J Biol Chem 1991, 266:15240-15243.
5. Sato T, Sakaguchi M, Mihara K, Omura T: The amino-terminal structures that determine topological orientation of cytochrome P-450 in microsomal membrane. EMBO J 1990, 9:2391-2397.
6. Sakaguchi M, Tomiyoshi R, Kuroiwa T, Mihara K, Omura T: Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge. Proc Natl Acad Sci USA 1992, 89:16-19.
7. Sakaguchi M: Mutational analysis of signal-anchor and stop-transfer sequences in membrane proteins. In Membrane Protein Assembly. Edited by von Heijne G. New York: Chapman and Hall; 1997:135-150.
8. Lyko F, Martoglio B, Jungnickel B, Rapoport TA, Dobberstein B: Signal sequence processing in rough microsomes. J Biol Chem 1995, 270:19873-19878.
9. Klappa P, Dierks T, Zimmermann R: Cyclosporin A inhibits the degradation of signal sequences after processing of presecretory proteins by signal peptidase. Eur J Biochem 1996, 239:509-518.
10. Fang H, Panzner S, Mullins C, Hartmann E, Green N: The homologue of mammalian SPC12 is important for efficient signal peptidase activity in Saccharomyces cerevisiae. J Biol Chem 1996, 271:16460-16465.
11. Mullins C, Meyer H-A, Hartmann E, Green N, Fang H: Structurally related Spc1p and Spc2p of yeast signal peptidase complex are functionally distinct J Biol Chem 1996, 271:29094-29099.
12. Walter P, Johnson AE: Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol 1994, 10:87-119.
13. Wiedmann B, Sakai H, Davis TA, Wiedmann M: A protein complex required for signal-sequence-specific sorting and translocation. Nature 1994, 370:434-440.
14. Lauring B, Kreibich G, Wiedmann M: The intrinsic ability of ribosomes to bind to endoplasmic reticulum membranes is regulated by signal recognition particle and nascent polypeptide-associated complex. Proc Natl Acad Sci USA 1995, 92:9435-9439.
15. Lauring B, Sakai H, Kreibich G, Wiedmann M: Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum. Proc Natl Acad Sci USA 1995, 92:5411-5415.
16. Powers T, Walter P: The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome. Curr Biol 1996, 6:331-338.
17. Bacher G, Lütcke H, Jungnickel B, Rapoport TA, Dobberstein B: Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting. Nature 1996, 381:248-251. This report demonstrates the function of ribosomes in the GTPase cycle of the signal recognition particle (SRP) and also clarifies the fate both of GTP and GDP forms of SRP in the protein targeting process.
18. Jungnickel B, Rapoport TA: A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 1995, 82:261-270.
19. Belin D, Bost S, Vassalli J-D, Strub K: A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J 1996, 15:468-478. This paper, together with [18], clearly demonstrates that signal sequences are recognized at other steps during translocation, in addition to recognition by signal recognition particles.
20. Freymann DM, Keenan RJ, Stroud RM, Walter P: Structure of the conserved GTPase domain of the signal recognition particle. Nature 1997, 385:361-364.
21. Montoya G, Svensson C, Luirink J, Sinning I: Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature 1997, 385:365-368.
22. Crowley KS, Liao S, Worrell VE, Reinhart GD, Johnson AE: Secretory proteins move through the ER membrane via an aqueous, gated pore. Cell 1994, 78:461-471.
23. Görlich D, Rapoport TA: Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 1993, 75:615-630.
24. Hartmann E, Sommer T, Prehn S, Görrich D, Jentsch S, Rapoport TA: Evolutionary conservation of components of the protein translocation complex. Nature 1994, 367:654-657.
25. Ito K: The major pathways of protein translocation across membranes. Genes Cells 1996, 1:337-346.
26. Voigt S, Jungnickel B, Hartmann E, Rapoport TA: Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane. J Cell Biol 1996, 134:25-35. It has been demonstrated that the signal peptide determines the requirement of TRAM proteins for in vitro translocation of a secretory protein. Systematic analysis of structure and TRAM-requirement relationship were described.
27. Nicchitta C, Murphy EC III, Haynes R, Shelness GS: Stage-and ribosome-specific alterations in nascent chain-Sec61p interactions accompany translocation across the ER membrane. J Cell Biol 1995, 129:957-970.
28. Do H, Falcone D, Lin J, Andrews DW, Johnson AE: The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 1996, 85:369-378. This paper demonstrates that, during the membrane anchoring of the transmembrane segment, the segment is released from the proximity of Sec61α to that of the TRAM protein. The nascent chain is maintained near the TRAM protein until the nascent chain is released from the ribosomes.
29. Borel AC, Simon SM: Biogenesis of polytopic membrane proteins: membrane segments assemble within translocation channels prior to membrane integration. Cell 1996, 85:379-389. This report demonstrates that multiple transmembrane segments in the growing nascent polypeptides exist in the aqueous environment of the translocation channel until the nascent chain is released from the ribosomes.
30. Hanein D, Matlack KE, Jungnickel B, Plath K, Kalies KU, Miller KR, Rapoport TA, Akey CW: Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell 1996, 87:721-732. This is the first structural view of the Sec61p complex, which forms a ring structure with a pore of 20 Å. Interestingly, the ring-like structures on the membrane were induced by the addition of ribosomes (for mammalian complex) or Sec62-63p complex (for yeast complex). Thus they most likely represent the protein conducting channel.
31. Nicchitta CV, Blobel G: Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation. Cell 1993, 73:989-998.
32. Dierks T, Volkmer J, Schlenstedt G, Jung C, Sandholzer U, Zachmann K, Schlotterhose P, Neifer K, Schmidt B, Zimmermann R: A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum. EMBO J 1996, 15:6931-6942. This paper indicates that ATP-binding factor(s) are involved in the efficient translocation of proteins across mammalian ER membrane in addition to Sec61p complex and TRAM protein. The authors suggest that the factor is likely to be GRP170 which is similar to Lhs1p, a genetically identified yeast protein translocation factor [33].
33. Craven RA, Egerton M, Stirling CJ: A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors. EMBO J 1996, 15:2640-2650.
34. Hegde RS, Lingappa VR: Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol. Cell 1996, 85:217-228.
35. Finke K, Plath K, Panzner S, Prehn S, Rapoport TA, Hartmann E, Sommer T: A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J 1996, 15:1482-1494. This paper demonstrates the existence of a second trimeric complex, which is highly homologous in sequence with the Sec61p trimeric complex. Although the complex is not essential for viability, it might provide a special cotranslational translocation pathway, which would become a useful tool for production of secretory recombinant proteins.
36. Rapoport TA, Rolls MM, Jungnickel B: Approaching the mechanism of protein transport across the ER membrane. Curr Opin Cell Biol 1996, 8:499-504.
37. Kuroiwa T, Sakaguchi M, Mihara K, Omura T: Systematic analysis of stop-transfer sequence for microsomal membrane. J Biol Chem 1991, 266:9251-9255.
38. Martoglio B, Hofmann M, Brunner J, Dobberstein B: The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 1995, 81:207-214.
39. Kuroiwa T, Sakaguchi M, Omura T, Mihara K: Reinitiation of protein translocation across the endoplasmic reticulum membrane for the topogenesis of multispanning membrane proteins. J Biol Chem 1996, 271:6423-6428.
40. Gafvelin G, Sakaguchi M, Andersson H, von Heijne G: Topological rules for membrane protein assembly in eukaryotic cells. J Biol Chem 1997, 272:6119-6127.
41. Corsi AK, Schekman R: Mechanism pf polypeptide translocation into the endoplasmic reticulum. J Biol Chem 1996, 271:30299-30302.
42. Rapoport TA, Jungnickel B, Kutay U: Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu Rev Biochem 1996, 65:271-303.
43. Panzner S, Dreier L, Hartmann E, Kostka S, Rapoport TA: Post-translational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 1995, 81:561-570.
44. Lyman SK, Schekman R: Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 1997, 88:85-96. In the post-translational targeting pathway, the authors clarified the functions of the subcomplex of Sec62-72-73p as a signal sequence receptor. The transfer of the secretory protein from the receptor to the Sec61p channel complex was, interestingly, induced by Sec63p and BiP interacting with the J-domain of Sec63p.
45. Hamilton TG, Flynn GC: Cer1p, a novel hsp70-related protein required for post-translational endoplasmic reticulum translocation in yeast J Biol Chem 1996, 271:30610-30613.
46. Ng DTW, Brown JD, Walter P: Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J Cell Biol 1996, 134:269-278. This paper clearly demonstrates that depending on the structural features of signal peptides, secretory proteins are differently targeted to the ER, namely into the cotranslational and/or post-translational pathways.
47. Reiss G, Hessen S, Gilmore R, Zufferey R, Aebi M: A specific screen for oligosaccharyltransferase mutations identifies the 9 kDa OST5 protein required for optimal activity in vivo and in vitro. EMBO J 1997, 16:1164-1172.
48. Shakin-Eshleman SH, Spitalnik SL, Kasturi L: The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency. J Biol Chem 1996, 271:6363-6366.
49. Gavel Y, von Heijne G: Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng 1990, 3:433-442.
50. Feng W, Matzuk MM, Mountjoy K, Bedows E, Ruddon RW: The asparagine-linked oligosaccharides of the human chorionic gonadotropin β subunit facilitate correct disulfide bond pairing. J Biol Chem 1995, 270:11851-11859.
51. Helenius A: How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol Biol Cell 1994, 5: 253-265.
52. Gething M-J, Sambrook J: Protein folding in the cell. Nature 1992, 355:33-45.
53. Ruddon RW, Bedows E: Assisted protein folding. J Biol Chem 1997, 272:3125-3128.
54. Marcus N, Shaffer D, Farrar P, Green M: Tissue distribution of three members of the murine protein disulfide isomerase (PDI) family. Biochim Biophys Acta 1996, 1309:253-260.
55. Melnick J, Dul JL, Argon Y: Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 1994, 370:373-375.
56. Kim PS, Arvan P: Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J Cell Biol 1995, 128:29-38.
57. Hammond C, Helenius A: Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 1994, 266:456-458.
58. Kuznetsov G, Bush KT, Zhang PL, Nigam SK: Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia. Proc Natl Acad Sci USA 1996, 93:8584-8589.
59. Otteken A, Moss B: Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J Biol Chem 1996, 271:97-103.
60. Feng W, Bedows E, Norton SE, Ruddon RW: Novel covalent chaperone complexes associated with human chorionic gonadotropin beta subunit folding intermediates. J Biol Chem 1996, 271:185431-18548.
61. Katsumi A, Senda T, Yamashita Y, Yamazaki T, Hamaguchi M, Kojima T, Kobayashi S, Saito H: Protein C Nagoya, an elongated mutant of protein C, is retained within the endoplasmic reticulum and is associated with GRP78 and GRP94. Blood 1996, 87:4164-4175.
62. Tokunaga F, Wakabayashi S, Koide T: Warfarin causes the degradation of protein C precursor in the endoplasmic reticulum. Biochemistry 1995, 34:1163-1170.
63. Tatu U, Helenius A: Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J Cell Biol 1997, 136:555-565. It was demonstrated that premature polypeptide interacting with calnexin is involved in a large complex, which consists of various chaperones and unknown ER proteins.
64. Kuznetsov G, Chen LB, Nigam SK: Multiple molecular chaperones complex with misfolded large oligomerlc glycoproteins in the endoplasmic reticulum. J Biol Chem 1997, 272:3057-3063.
65. Hebert DN, Foellmer B, Helenius A: Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 1995, 81:425-433.
66. Hammond C, Helenius A: Quality control in the secretory pathway. Curr Opin Cell Biol 1995, 7:523-529.
67. Van Leeuwen JEM, Kearse KP: Reglucosylation of N-linked glycans is critical for calnexin assembly with T cell receptor (TCR) α proteins but not TCRβ proteins. J Biol Chem 1997, 272: 4179-4186.
68. Rodan AR, Simons JF, Trombetta ES, Helenius A: N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO J 1996, 15:6921-6930.
69. Zapun A, Petrescu SM, Rudd PM, Dwek RA, Thomas DY, Bergeron JJ: Conformation-independent binding of monoglucosylated ribonuclease B to calnexin. Cell 1997, 88:29-38. The authors provide evidence to support the hypothesis that calnexin functions solely as a lectin. Calnexin interacts with the monoglucosylated mannose-core glycan of ribonuclease B irrespective of the folding state of the protein moiety.
70. Helenius A, Trombetta ES, Hebert DN, Simons JF: Calnexin, calreticulin and the folding of glycoproteins. Trends Cell Biol 1997, 7:193-200.
71. Hebert DN, Foellmer B, A. H: Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J 1996, 15:2961-2968.
72. Cannon KS, Hebert DN, Helenius A: Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin. J Biol Chem 1996, 271:14280-14284.
73. Vassilakos A, Cohen-Doyle MF, Peterson PA, Jackson MR, Williams DB: The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J 1996, 15:1495-1506.
74. Hiller MM, Finger A, Schweiger M, Wolf DH: ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 1996, 273:1725-1728.
75. Brodsky JL, McCracken AA: ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol 1997, 7:151-156. This review covers recent progress in the study of degradation of ER-retained proteins.
76. Kopito RR: ER quality control: the cytoplasmic connection. Cell 1997, 88:427-430.
77. Wiertz EJ, Tortorella D, Bogyo M, Yu J, Mothes W, Jones TR, Rapoport TA, Ploegh HL: Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 1996, 384:432-438.