Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

Cell

Volumn 87, Issue 4, 1996, Pages 721-732

  Hanein, Dorit ^a   Matlack, Kent E S ^b   Jungnickel, Berit ^b   Plath, Kathrin ^b,c   Kalies, Kai Uwe ^c   Miller, Kenneth R ^d   Rapoport, Tom A ^b   Akey, Christopher W ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^d BROWN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; ELECTRON MICROSCOPY; ENDOPLASMIC RETICULUM; GENE TRANSLOCATION; HYDROPHOBICITY; LIGAND BINDING; MAMMAL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROCESSING; PROTEOLIPOSOME; RIBOSOME; YEAST;

MAMMALIA;

EID: 0345444027     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81391-4     Document Type: Article

References (38)

1. Akey, C.W. (1995). Structural plasticity of the nuclear pore complex. J. Mol. Biol. 248, 273-293.
2. Belin, D., Bost, S., Vassalli, J.-D., and Strub, K. (1996). A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J. 15, 468-478.
3. Blobel, G., and Dobberstein, B. (1975). Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J. Cell Biol. 67, 852-862.
4. Crowley, K.S., Reinhart, G.D., and Johnson, A.E. (1993). The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell 73, 1101-1115.
5. Crowley, K.S., Liao, S.R., Worrell, V.E., Reinhart, G.D., and Johnson, A.E. (1994). Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78, 461-471.
6. Deshaies, R.J., and Kirschner, M. (1995). G1 cyclin-dependent activation of p34CDC28 (Cdc28p) in vitro. Proc. Natl. Acad. Sci. USA 92, 1182-1186.
7. Deshaies, R.J., and Schekman, R. (1987). A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J. Cell Biol. 105, 633-645.
8. 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.
9. Dubochet, J., Adrian, M., Chang, J.-J., Homo, J.-C., Lepault, J., McDowall, A.W., and Schultz, P. (1988). Cryo-electron microscopy of vitrified specimens. Q. Rev. Biophys. 21, 129-228.
10. Finke, K., Plath, K., Panzner, S., Prehn, S., Rapoport, T.A., Hartmann, E., and Sommer, Th. (1996). A second trimeric complex containing homologs of the Sec61 p-complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J. 15, 1482-1494.
11. Frank, J., Bretaudiere, J.-P., Carazo, J.-M., Verschoor, A., and Wagenknecht, T. (1988). Classification of images of biomolecular assemblies: a study of ribosomes and ribosomal subunits of Escherichia coli. J. Microscopy 150, 99-115.
12. Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., and Leith, A. (1996). SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199.
13. Giddings, T.H., and Staehelin, L.A. (1980). Ribosome binding sites visualized on freeze-fractured membranes of the rough endoplasmic reticulum. J. Cell Biol. 85, 147-152.
14. Görlich, D., Prehn, S., Hartmann, E., Kalies, K.U., and Rapoport, T.A. (1992). A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation. Cell 71, 489-503.
15. Görlich, D., and Rapoport, T.A. (1993). Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75, 615-630.
16. Hartmann, E., Sommer, T., Prehn, S., Görlich, D., Jentsch, S., and Rapoport, T.A. (1994). Evolutionary conservation of components of the protein translocation complex. Nature 367, 654-657.
17. High, S., Andersen, S.S.L., Görlich, D., Hartmann, E., Prehn, S., Rapoport, T.A., and Dobberstein, B. (1993). Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion. J. Cell Biol. 121, 743-750.
18. Jungnickel, B., and Rapoport, T.A. (1995). A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270.
19. Kalies, K.U., Görlich, D., and Rapoport, T.A. (1994). Binding of ribosomes to the rough endoplasmic reticulum mediated by the sec61p-complex. J. Cell Biol. 126, 925-934.
20. Kellaris, K.V., Bowen, S., and Gilmore, R. (1991). ER translocation intermediates are adjacent to a nonglycosylated 34-kD integral membrane protein. J. Cell Biol. 114, 21-33.
21. Kutay, U., Ahnert-Hilger, G., Hartmann, E., Wiedenmann, B., and Rapoport, T.A. (1995). Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. EMBO J. 14, 217-223.
22. 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.
23. Mothes, W., Prehn, S., and Rapoport, T.A. (1994). Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. EMBO J. 13, 3937-3982.
24. Müsch, A., Wiedmann, M., and Rapoport, T.A. (1992). Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane. Cell 69, 343-352.
25. Nicchitta, C.V., Murphy, E.C.R., Haynes, R., and Shelness, G.S. (1995). Stage-and ribosome-specific alterations in nascent chain-Sec61p interactions accompany translocation across the ER membrane. J. Cell Biol. 129, 957-970.
26. Ojakian, G.K., Kreibich, G., and Sabatini, D.D. (1977). Mobility of ribosomes bound to microsomal membranes. A freeze-etch and thin-section electron microscope study of the structure and fluidity of the rough endoplasmic reticulum. J. Cell Biol. 72, 530-551.
27. Panzner, S., Dreier, L., Hartmann, E., Kostka, S., and Rapoport, T.A. (1995). Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81, 561-570.
28. Rapoport, T.A. (1985). Extensions of the signal hypothesis -sequential insertion model versus amphipathic tunnel hypothesis. FEBS Lett. 187, 1-10.
29. 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.
30. Rothblatt, J.A., Deshaies, R.J., Sanders, S.L., Daum, G., and Schekman, R. (1989). Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell Biol. 109, 2641-2652.
31. 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.
32. Simon, S.M., and Blobel, G. (1991). A protein-conducting channel in the endoplasmic reticulum. Cell 65, 371-380.
33. Singer, S., Maher, P., and Yaffe, M. (1987). On the transfer of integral proteins into membranes. Proc. Natl. Acad. Sci. USA 84, 1960-1964.
34. Strambio-de-Castillia, C., Blobel, G., and Rout, M.P. (1995). Isolation and characterization of nuclear envelopes from the yeast Saccharomyces. J. Cell Biol. 131, 19-31.
35. Wall, J.S., and Hainfeld, J.F. (1986). Mass mapping with the scanning transmission electron microscope. Annu. Rev. Biophys. Biophys. Chem. 15, 355-376.
36. Walter, P., and Blobel, G. (1983). Preparation of microsomal membranes for cotranslational protein translocation. Meth. Enzymol. 96, 84-93.
37. 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.
38. Walter, P., Ibrahimi, I., and Blobel, G. (1981). Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in vitro assembled polysomes synthesizing secretory protein. J. Cell Biol. 91, 545-550.