Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP

Cell

Volumn 88, Issue 1, 1997, Pages 85-96

  Lyman, Susan K ^a,b   Schekman, Randy ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HEAT SHOCK PROTEIN 70; PROTEIN PRECURSOR; SECRETORY PROTEIN; SIGNAL PEPTIDE;

ARTICLE; ENDOPLASMIC RETICULUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; PROTEIN TRANSPORT;

EID: 0030970268     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81861-9     Document Type: Article

References (51)

1. Allison, D.S., and Young, E.T. (1988). Single-amino-acid substitutions within the signal sequence of yeast prepro-α-factor affect membrane translocation. Mol. Cell. Biol. 8, 1915-1922.
2. Allison, D.S., and Young, E.T. (1989). Mutations in the signal sequence of prepro-α-factor inhibit both translocation into the endoplasmic reticulum and processing by signal peptidase in yeast cells. Mol. Cell. Biol. 9, 4977-4985.
3. Bird, P., Gething, M., and Sambrook, J. (1987). Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent. J. Cell Biol. 105, 2905-2914.
4. Brodsky, J.L. (1996). Post-translational translocation: not all hsc70s are created equal. Trends Biochem. Sci. 21, 122-126.
5. Brodsky, J.L., Goeckeler, J., and Schekman, R. (1995). BiP and Sec63p are required for both co-and post-translational protein translocation into the yeast endoplasmic reticulum. Proc. Natl. Acad. Sci. 92, 9643-9646.
6. Brodsky, J.L., Hamamoto, S., Feldheim, D., and Schekman, R. (1993). Reconstitution of protein translocation from solubilized yeast membranes reveals topologically distinct roles for BiP and cytosolic hsc70. J. Cell Biol. 120, 95-102.
7. Brodsky, J.L., and Schekman, R. (1993). A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J. Cell Biol. 123, 1355-1363.
8. Brodsky, J.L., and Schekman, R. (1994). Heat shock cognate proteins and polypeptide translocation across the endoplasmic reticulum membrane. In The Biology of Heat Shock Proteins and Molecular Chaperones, Morimoto, R.I., Tissieres, A., and Georgopoulos, C., eds. (Plainview, New York: Cold Spring Harbor Laboratory Press), pp. 85-109.
9. Caplan, A.J., Cyr, D.M., and Douglas, M.G. (1993). Eukaryotic homologues of Escherichia coli DnaJ: a diverse protein family that functions with hsp70 stress proteins. Mol. Biol. Cell 4, 555-563.
10. Crowley, K.S., Liao, S., 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.
11. Cyr, D.M., Langer, T., and Douglas, M.G. (1994). DnaJ-like proteins: molecular chaperones and specific regulators of hsp70. Trends Biochem. Sci. 19, 176-181.
12. Deshaies, R.J., Sanders, S.L., Feldheim, D.A., and Schekman, R. (1991). Assembly of the yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisub-unit complex. Nature 349, 806-808.
13. Deshaies, R.J., and Schekman, R. (1990). Structural and functional dissection of Sec62p, a membrane-bound component of the yeast endoplasmic reticulum protein import machinery. Mol. Cell Biol. 10, 6024-6035.
14. Deshaies, R.J., and Schekman, R.W. (1989). SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum. J. Cell Biol. 109, 2653-2664.
15. Fang, H., and Green, N. (1994). Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63-BiP complex from S. cerevisiae. Mol. Biol. Cell 5, 933-942.
16. 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.
17. Feldheim, D., and Schekman, R. (1994). Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J. Cell Biol. 126, 935-943.
18. Feldheim, D., Yoshimura, K., Admon, A., and Schekman, R. (1993). Structural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum. Mol. Biol. Cell 4, 931-939.
19. Glick, B.S. (1995). Can hsp70 proteins act as force-generating motors? Cell 80, 11-14.
20. Görlich, D., and Rapoport, T.A. (1993). Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75, 615-630.
21. Hansen, W., Garcia, P.D., and Walter, P. (1986). In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent post-translational translocation of the prepro-α-factor. Cell 45, 397-406.
22. Hansen, W., and Walter, P. (1988). Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae. J. Cell Biol. 106, 1075-1081.
23. Hightower, L.E., Sadis, S.E., and Takenaka, I.M. (1994). Interaction of vertebrate hsc70 and hsp70 with unfolded proteins and peptides. In The Biology of Heat Shock Proteins and Molecular Chaperones, Morimoto, R.I., Tissieres, A., and Georgopoulos, C., eds. (Plainview, New York: Cold Spring Harbor Laboratory Press), pp. 179-207.
24. Jungnickel, B., and Rapoport, T.A. (1995). A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270.
25. Krieg, U.C., Johnson, A.E., and Walter, P. (1989). Protein translocation across the endoplasmic reticulum membrane: identification by photo-cross-linking of a 39kD integral membrane glycoprotein as part of a putative translocation tunnel. J. Cell Biol. 109, 2033-2043.
26. Kurihara, T., and Silver, P. (1993). Suppression of a sec63 mutation identifies a novel component of the yeast endoplasmic reticulum translocation apparatus. Mol. Biol. Cell 4, 919-930.
27. Lyman, S.K. (1996) I. Heat shock protein function in the initiation of bacteriophage lambda replication. II. Molecular dissection of protein translocation into the ER of S. cerevisiae. Phd Thesis, University of California, Berkeley, California.
28. Lyman, S.K., and Schekman, R. (1995). Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae. J. Cell Biol. 131, 1163-1171.
29. Lyman, S.K., and Schekman, R. Protein translocation into the endoplasmic reticulum. In Guidebook to Molecular Chaperones and Protein Folding Catalysts, Gething, M.-J., ed. (Oxford University Press), in press.
30. 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 13, 3973-3982.
31. Müsch, A., Wiedmann, M., and Rapoport, T.A. (1992). Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane. Cell 69, 343-352.
32. Nelson, M.K., Kurihara, T., and Silver, P.A. (1993). Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae. Genetics 134, 159-173.
33. Ng, D.T. W., Brown, J.D., and Walter, P. (1996). Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J. Cell Biol. 134, 269-278.
34. Nguyen, T.H., Law, D.T.S., and Williams, D.B. (1991). Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. 88, 1565-1569.
35. Ogg, S.C., Poritz, M.A., and Walter, P. (1992). Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae. Mol. Biol. Cell 3, 895-911.
36. 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.
37. Rose, M.D., Misra, L.M., and Vogel, J.P. (1989). KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57, 1211-1221.
38. 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.
39. Rothblatt, J.A., and Meyer, D.I. (1986). Secretion in yeast: reconstitution of the translocation and glycosylation of α-factor and invertase in a homologous cell-free system. Cell 44, 619-628.
40. Sadler, I., Chiang, A., Kurihara, T., Rothblatt, J., Way, J., and Silver, P. (1989). A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein. J. Cell Biol. 109, 2665-2675.
41. 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.
42. Sanz, P., and Meyer, D.I. (1989). Secretion in yeast: preprotein binding to a membrane receptor and ATP-dependent translocation are sequential and separable events in vitro. J. Cell Biol. 108, 2101-2106.
43. Scidmore, M.A., Okamura, H.H., and Rose, M.D. (1993). Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum. Mol. Biol. Cell 4, 1145-1159.
44. 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.
45. Vogel, J.P., Misra, L.M., and Rose, M.D. (1990). Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J. Cell Biol. 110, 1885-1895.
46. 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.
47. Waters, M.G., and Blobel, G. (1986a). Prepro-α-factor has a cleavable signal sequence. J. Biol. Chem. 263, 6209-6214.
48. Waters, M.G., and Blobel, G. (1986b). Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis. J. Cell Biol. 102, 1543-1550.
49. Wei, J., Gaut, J.R., and Hendershot, L.M. (1995). In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis. J. Biol. Chem. 270, 26677-26682.
50. Wickner, W.T. (1994). How ATP drives proteins across membranes. Science 266, 1197-1198.
51. Wiedmann, M., Görlich, D., Hartmann, E., Kurzchalia, T.V., and Rapo-port, T. (1989). Photo-cross-linking demonstrates proximity of a 34 kD membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum. FEBS Lett. 257, 263-268.