Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity

Molecular Biology of the Cell

Volumn 11, Issue 1, 2000, Pages 217-226

  Chillarón, Josep ^a   Haas, Ingrid G ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN LIGHT CHAIN; PROTEASOME;

ANIMAL CELL; ARTICLE; CELL FRACTIONATION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; IMMUNOGLOBULIN STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE;

ANIMALIA;

EID: 0033957668     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.1.217     Document Type: Article

References (56)

1. Beggah, A., Mathews, P., Beguin, P., and Geering, K. (1996). Degradation and endoplasmic reticulum retention of unassembled alpha and beta subunits of Na, K ATPase correlate with interaction of BiP. J. Biol. Chem. 271, 20895-20902.
2. Biederer, T., Volkwein, C., and Sommer, T. (1997). Role of Cue1p in ubiquitination and degradation at the ER surface. Science 278, 1806-1809.
3. Bordallo, J., Plemper, R.K., Finger, A., and Wolf, D.H. (1998). Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol. Biol. Cell 9, 209-222.
4. Brodsky, J.L., and McCracken, A.A. (1997). ER associated and proteasome mediated protein degradation: How two topologically restricted events came together. Trends Cell Biol. 7, 151-156.
5. Brodsky, J.L., Werner, E.D., Dubas, M.E., Goeckeler, J.L., Kruse, K.B., and McCracken, A.A. (1999). The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274, 3453-3460.
6. Bush, K.T., Goldberg, A.L., and Nigam, S.K. (1997). Proteasome inhibition leads to a heat shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J. Biol. Chem. 272, 9086-9092.
7. Corsi, A.K., and Schekman, R. (1997). 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.
8. Cremer, A., Knittler, M.R., and Haas, I.G. (1994). Biosynthesis of antibodies and molecular chaperones. In: Forty-fourth Colloquim Mosbach, ed. F. Wieland and W. Reutter, Berlin: Springer, 171-184.
9. deVirgilio, M., Weninger, H., and Ivessa, N.E. (1998). Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J. Biol. Chem. 273, 9734-9743.
10. Dusseljee, S., Wubbolts, R., Verwoerd, D., Tulp, A., Janssen, H., Calafat, J., and Neefjes, J. (1998). Removal and degradation of the free MHC class II beta chain in the endoplasmic reticulum requires proteasomes and is accelerated by BFA. J. Cell Sci. 15, 2217-2226.
11. Enenkel, C., Lehmann, A., and Kloetzel, P.M. (1998). Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope ER network in yeast. EMBO J. 17, 6144-6154.
12. Fenteany, G., and Schreiber, S.L. (1998). Lactacystin, proteasome function, and cell fate. J. Biol. Chem. 273, 8545-8548.
13. Gardner, A.M., Aviel, S., and Argon, Y. (1993). Rapid degradation of an unassembled immunoglobulin light chain is mediated by a serine protease and occurs in a preGolgi compartment. J. Biol. Chem. 268, 25940-25947.
14. Glickman, M.H., Rubin, D.M., Fried, V.A., and Finley, D. (1998). The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. 18, 3149-3162.
15. Hamman, B.D., Hendershot, L.M., and Johnson, A.E. (1998). BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92, 747-758.
16. Hammond, C., and Helenius, A. (1995). Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7, 523-529.
17. Hampton, R.Y., Gardner, R.G., and Rine, J. (1996). Role of 26S proteasome and HRD genes in the degradation of 3 hydroxy 3 methylglutaryl CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7, 2029-2044.
18. Hellman, R., Vanhove, M., Lejeune, A., Stevens, F.J., and Hendershot, L.M. (1999). The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. J. Cell Biol. 144, 21-30.
19. Hiller, M.M., Finger, A., Schweiger, M., and Wolf, D.H. (1996). ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-1728.
20. Hughes, E.A., Hammond, C., and Cresswell, P. (1997). Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc. Natl. Acad. Sci. USA 94, 1896-1901.
21. Huppa, J.B., and Ploegh, H.L. (1997). The alpha chain of the T cell antigen receptor is degraded in the cytosol. Immunity 7, 113-122.
22. Ivessa, N.E., Kitzmüller, C., and de Virgilio, M. (1999). ER-associated protein degradation inside and outside of the endoplasmic reticulum. Protoplasma (in press).
23. Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L., and Riordan, J.R. (1995). Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-135.
24. Keller, S.H., Lindstrom, J., and Taylor, P. (1998). Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor. J. Biol. Chem. 273, 17064-17072.
25. Kessler, S.W. (1975). Rapid isolation of antigens from cells with a staphylococcal protein A-antibody adsorbent: parameters of the interaction of antibody-antigen complexes with protein A. J. Immunol. 115, 1617-1624.
26. Knittler, M.R., Dirks, S., and Haas, I.G. (1995). Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92, 1764-1768.
27. Knittler, M.R., and Haas, I.G. (1992). Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release. EMBO J. 11, 1573-1581.
28. Knop, M., Finger, A., Braun, T., Hellmuth, K., and Wolf, D.H. (1996a). Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 15, 753-763.
29. Knop, M., Hauser, N., and Wolf, D.H. (1996b). N-glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12, 1229-1238.
30. Köhler, G., Howe, S.C., and Milstein, C. (1976). Fusion between immunoglobulin-secreting and nonsecreting myeloma cell lines. Eur. J. Immunol. 6, 292-295.
31. Kopito, R.R. (1997). ER quality control: the cytoplasmic connection. Cell 88, 427-430.
32. Lee, D.H., and Goldberg, A.L. (1998). Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8, 397-403.
33. Leitzgen, K., and Haas, I.G. (1998). Protein maturation in the ER. Chemtracts 11, 423-445.
34. Leonhard, K., Stiegler, A., Neupert, W., and Langer, T. (1999). Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease. Nature 398, 348-351.
35. Liu, Y., Choudhury, P., Cabral, C.M., and Sifers, R.N. (1997). Intracellular disposal of incompletely folded human alpha(1) antitrypsin involves release from calnexin and post translational trimming of asparagine linked oligosaccharides. J. Biol. Chem. 272, 7946-7951.
36. Mathew, A., Mathur, S.K., and Morimoto, R.I. (1998). Heat shock response and protein degradation: regulation of HSF2 by the ubiquitin-proteasome pathway. Mol. Cell. Biol. 18, 5091-5098.
37. Mayer, T.U., Braun, T., and Jentsch, S. (1998). Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO J. 17, 3251-3257.
38. McCracken, A.A., and Brodsky, J.L. (1996). Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132, 291-298.
39. Meerovitch, K., Wing, S., and Goltzman, D. (1998). Proparathyroid hormone-related protein is associated with the chaperone protein BiP and undergoes proteasome-mediated degradation. J. Biol. Chem. 273, 21025-21030.
40. Pilon, M., Schekman, R., and Romisch, K. (1997). Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16, 4540-4548.
41. Plemper, R.K., Bohmler, S., Bordallo. J., Sommer, T., and Wolf, D.H. (1997). Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388, 891-895.
42. Plemper, R.K., Deak, P.M., Otto, R.T., and Wolf, D.H. (1999). Reentering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. FEBS Lett. 443, 241-245.
43. Plemper, R.K., Egner, R., Kuchler, K., and Wolf, D.H. (1998). Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome. J. Biol. Chem. 273, 32848-32856.
44. Qu, D.F., Teckman, J.H., Omura, S., and Perlmutter, D.H. (1996). Degradation of a mutant secretory protein, alpha(1)-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 271, 22791-22795.
45. Rivett, A.J. (1998). Intracellular distribution of proteasomes. Curr. Opin. Immunol. 10, 110-114.
46. Skowronek, M.H., Hendershot, L.M., and Haas, I.G. (1998). The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proc. Natl. Acad. Sci. USA 95, 1574-1578.
47. Skowronek, M.H., Rotter, M., and Haas, I.G. (1999). Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog. Biol. Chem. 380, 1133-1138.
48. Sommer, T., and Wolf, D.H. (1997). Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J. 11, 1227-1233.
49. Tortorella, D., Story, C.M., Huppa, J.B., Wiertz, E.J., Jones, T.R., and Ploegh, H.L. (1998). Dislocation of type 1 membrane proteins from the ER to the cytosol is sensitive to changes in redox potential. J. Cell Biol. 142, 365-376.
50. Ward, C.L., Omura, S., and Kopito, R.R. (1995). Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127.
51. Wehland, J., and Weber, K. (1987). Turnover of the carboxy-terminal tyrosine of alpha-tubulin and means of reaching elevated levels of detyrosination in living cells. J. Cell Sci. 88, 185-203.
52. Werner, E.D., Brodsky, J.L., and McCracken, A.A. (1996). Proteasome dependent endoplasmic reticulum associated protein degradation: an unconventional route to a familiar fate. Proc. Natl. Acad. Sci. USA 93, 13797-13801.
53. Wiertz, E., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T.R., Rapoport, T.A., and Ploegh, H.L. (1996a). Sec61 mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438.
54. Wiertz, E.J., Jones, T.R., Sun, L., Bogyo, M., Geuze, H.J., and Ploegh, H.L. (1996b). The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84, 769-779.
55. Yang, M., Omura, S., Bonifacino, J.S., and Weissman, A.M. (1998). Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J. Exp. Med. 187, 835-846.
56. Yu, H., Kaung, G., Kobayashi, S., and Kopito, R.R. (1997). Cytosolic degradation of T cell receptor alpha chains by the proteasome. J. Biol. Chem. 272, 20800-20804.