Role of ribosome and translocon complex during folding of influenza hemagglutinin in the endoplasmic reticulum of living cells

Molecular Biology of the Cell

Volumn 11, Issue 2, 2000, Pages 765-772

  Chen, Wei ^a,c   Helenius, Ari ^b  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b ETH ZURICH   (Switzerland)

^c ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ; MEMBRANE PROTEIN; RIBOSOME DNA; TRANSLOCON; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ENDOPLASMIC RETICULUM; INFLUENZA VIRUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN TRANSPORT; RIBOSOME; SEMLIKI FOREST ALPHAVIRUS; VIRUS INFECTIVITY;

EID: 0033998246     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.2.765     Document Type: Article

References (27)

1. Beckmann, R.P., Mizzen, L.A., and Welch, W.J. (1990). Interaction of hsp70 with newly synthesized proteins: implications for folding and assembly. Science 248, 850-853.
2. 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.
3. Bukau, B., and Horwich, A.L. (1998). The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366.
4. Chen, W., Helenius, J., Braakman, I., and Helenius, A. (1995). Co-translational folding and calnexin binding of influenza hemagglutinin in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92, 6229-6233.
5. 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.
6. Fedorov, A.N., and Baldwin, T.O. (1997). Cotranslational protein folding. J. Biol. Chem. 272, 32715-32718.
7. Frand, A.R., and Kaiser, C.A. (1998). The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1, 161-170.
8. Freedman, R.B. (1989). Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell 57, 1069-1072.
9. Hamman, B.D., Chen, J.C., Johnson, E.E., and Johnson, A.E. (1997). The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane. Cell 89, 535-544.
10. Hammond, C., Braakman, I., and Helenius, A. (1994). Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 91, 913-917.
11. Hardesty, B., Tsalkova, T., and Kramer, G. (1999). Cotranslational folding. Curr. Opin. Struct. Biol. 9, 111-114.
12. 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.
13. Hurtley, S.M., Bole, D.G., Hoover-Litty, H., Helenius, A., and Copeland, C.S. (1989). Interactions of misfolded Influenza hemagglutinin with binding protein (BiP). J. Cell Biol. 108, 2117-2126.
14. Liljeström, P., and Garoff, H. (1991). A new generation of animal cell expression vectors based on the Semliki Forest virus replicon. Biotechnology 9, 1-7.
15. 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.
16. Molinari, M., and Helenius, A. (1999). Glycoproteins form mixed disulfides with oxidoreductases during folding in living cells. Nature 402, 90-93.
17. Mothes, W., Heinrich, S.U., Graf, R., Nilsson, I., von, H.G., Brunner, J., and Rapoport, T.A. (1997). Molecular mechanism of membrane protein integration into the endoplasmic reticulum. Cell 89, 523-533.
18. Nathans, D. (1964). Puromycin inhibition of protein synthesis: incorporation of puromycin into peptide chains. Proc. Natl. Acad. Sci. USA 51, 585-592.
19. Netzer, W.J., and Hartl, F.U. (1998). Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms. Trends Biochem. Sci. 23, 68-73.
20. Peterson, J.R., Ora, A., Nguyen Van, P., and Helenius, A. (1995). Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell 6, 1173-1184.
21. Rapoport, T.A., Jungnickel, B., and Kutay, U. (1996). Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271-303.
22. Singh, I., Doms, R.W., Wagner, K.R., and Helenius, A. (1990). Intracellular transport of soluble and membrane-bound glycoproteins: folding, assembly and secretion of anchor-free influenza hemagglutinin. EMBO J. 9, 631-639.
23. Strickland, D.K., Ashcom, J.D., Williams, S., Battey, F., Behre, E., McTigue, K., Battey, J.F., and Argraves, W.S. (1991). Primary structure of α2-macroglobulin receptor-associated protein. J. Biol. Chem. 266, 13364-13369.
24. Tatu, U., Hammond, C., and Helenius, A. (1995). Folding and oligomerization of Influenza hemagglutinin in the ER and the intermediate compartment. EMBO J. 34, 1340-1348.
25. Wettstein, F.O., Noll, H., Penman, S. (1964). Effect of cycloheximide on ribosomal aggregates engaged in protein synthesis in vitro. Biochim. Biophys. Acta 87, 525-528.
26. Whitley, P., Nilsson, I., and von Heijne, G. (1996). A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain. J. Biol. Chem. 271, 6241-6244.
27. Wilson, I.A., Skehel, J.J., and Wiley, D.C. (1981). Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289, 366-373.