Mutant analysis links the translocon and BIP to retrograde protein transport for ER degradation

Nature

Volumn 388, Issue 6645, 1997, Pages 891-895

  Plemper, Richard K ^a   Böhmler, Sigrun ^a   Bordallo, Javier ^a   Sommer, Thomas ^b   Wolf, Dieter H ^a  

^a UNIVERSITY OF STUTTGART   (Germany)

^b MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHAPERONE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MUTANT PROTEIN; PROTEASOME; SERINE CARBOXYPEPTIDASE;

ARTICLE; CYTOPLASM; CYTOSOL; ENDOPLASMIC RETICULUM; FUNGUS MUTANT; IMMUNOPRECIPITATION; INTRACELLULAR TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN TARGETING; PROTEIN TRANSPORT; YEAST;

BIOLOGICAL TRANSPORT; CARBOXYPEPTIDASES; ENDOPLASMIC RETICULUM; FUNGAL PROTEINS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; LIGASES; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; MUTATION; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN-CONJUGATING ENZYMES;

EUKARYOTA; FUNGI;

EID: 1842409617     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/42276     Document Type: Article

References (29)

1. Pryer, N. K., Wuestehube, L J. & Schekman, R. Vesicle-mediated protein sorting. Annu. Rev. Biochem. 61, 471-516 (1992).
2. Gething, M. J. & Sambrook, J. Protein folding in the cell. Nature 355, 33-45 (1992).
3. Kopito, R. R. ER quality control: the cytoplasmic connection. Cell 88, 427-430 (1997).
4. Biederer, T., Volkwein, C. & Sommer, T. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15, 2069-2076 (1996).
5. Hiller, M. M., Finger, A., Schweiger, M. & Wolf, D. H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-1728 (1996).
6. Werner, E. D., Brodsky, J. L. & McCracken, A. A. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc. Natl Acad. Sci. USA 93, 13797-13801 (1996).
7. Jensen, T. J. et al. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-135 (1995).
8. Halaban, R. et al. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc. Natl Acad. Sci. USA 94, 6210-6215 (1997).
9. Walter, P. & Johnson, A. E. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10, 87-119 (1994).
10. Rapoport, T. A., Jungnickel, B. & Kutay, U. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271-303 (1996).
11. Wiertz, E. J. H. J. et al. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438 (1996).
12. Lyman, S. K. & Schekman, R. Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88, 85-96 (1997).
13. Finger, A., Knop, M. & Wolf, D. H. Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur. J. Biochem. 218, 565-574 (1993).
14. Stirling, C. S., Rothblatt, J., Hosobuchi, M., Deshaies, R. & Schekman, R. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Cell. Biol. 3, 129-142 (1992).
15. Panzner, S., Dreier, L., Hartmann, E., Kostka, S. & Rapoport, T. A. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81, 561-570 (1995).
16. Finke, K. et al. A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J 15, 1482-1494 (1996).
17. Feldheim, D., Rothblatt, J. & Schekman, R. Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol. Cell. Biol. 12, 3288-3296 (1992).
18. Corsi, A. K. & Schekman, R. The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J. Cell Biol. 137, 1483-1493 (1997).
19. Cyr, D. M., Langer, T. & Douglas, M. G. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19, 176-181 (1994).
20. Hanein, D. et al. Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell 87, 721-732 (1996).
21. Scidmore, M. A., Okamura, H. H. & Rose, M. D. Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum. Mol. Biol. Cell 4, 1145-1159 (1993).
22. Sanders, S. L., Whitfield, K. M., Vogel, J. P., Rose, M. D. & Schekman, R. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell 69, 353-365 (1992).
23. Esnault, Y., Blondel, M.-O., Deshaies, R. J., Schekman, R. & Képès, F. The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum. EMBO J. 12, 4083-4093 (1993).
24. Ng, D. T., Brown, J. D. & Walter, P. Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J. Cell Biol. 134, 269-278 (1996).
25. Chen, P., Johnson, P., Sommer, T., Jentsch, S. & Hochstrasser, M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT α2 repressor Cell 74, 357-369 (1993).
26. Knop, M., Finger, A., Braun, T., Hellmuth, K. & Wolf, D. H. Der1, a novel protein specifically requires for endoplasmic reticulum degradation in yeast. EMBO J. 15, 753-763 (1996).
27. Hampton, R. Y., Gardner, R. G. & Rine, J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methyiglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7, 2029-2044 (1994).
28. Ausubel, F. M. et al. Current Protocols in Molecular Biology (Greene, New York, 1992).
29. Rose, M. D., Misra, L. M. & Vogel, J. P. Kar2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57, 1211-1221 (1989).