Endoplasmic reticulum quality control of asialoglycoprotein receptor H2a involves a determinant for retention and not retrieval

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 21, 1997, Pages 11363-11368

  Shenkman, Marina ^a   Ayalon, Michal ^a   Lederkremer, Gerardo Z ^a  

^a TEL AVIV UNIVERSITY   (Israel)

Author keywords

Endoplasmic reticulum degradation; Protein folding; Retention signal; Signal peptidase; T cell antigen receptor

Indexed keywords

ASIALOGLYCOPROTEIN RECEPTOR; CALNEXIN; NOCODAZOLE;

ARTICLE; ENDOPLASMIC RETICULUM; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN LOCALIZATION;

3T3 CELLS; AMINO ACID SEQUENCE; ANIMALS; ASIALOGLYCOPROTEIN RECEPTOR; BREFELDIN A; CALCIUM-BINDING PROTEINS; CALNEXIN; CARBOHYDRATE SEQUENCE; CELL MEMBRANE; CYCLOPENTANES; ENDOPLASMIC RETICULUM; GOLGI APPARATUS; HUMANS; MACROMOLECULAR SUBSTANCES; MICE; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NOCODAZOLE; PEPTIDE FRAGMENTS; PROTEIN FOLDING; RECEPTORS, CELL SURFACE; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SWAINSONINE; TRANSFECTION;

EID: 0030803232     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.21.11363     Document Type: Article

References (49)

1. Klausner, R. D. & Sitia, R. (1990) Cell 62, 611-614.
2. Hammond, C. & Helenius, A. (1995) Curr. Opin. Cell Biol. 7, 523-529.
3. Lippincott, S. J., Bonifacino, J. S., Yuan, L. C. & Klausner, R. D. (1988) Cell 54, 209-220.
4. Amara, J. F., Lederkremer, G. & Lodish, H. F. (1989) J. Cell Biol. 109, 3315-3324.
5. Kopito, R. R. (1997) Cell 88, 427-430.
6. Wileman, T., Carson, G. R., Shih, F. F., Concino, M. F. & Terhorst, C. (1990) Cell Regul. 1, 907-919.
7. Bonifacino, J. S., Suzuki, C. K. & Klausner, R. D. (1990) Science 247, 79-82.
8. Kumagai, H., Chun, K. T. & Simoni, R. D. (1995) J. Biol. Chem. 270, 19107-19113.
9. Foletti, D., Guerini, D. & Carafoli, E. (1995) FASEB J. 9, 670-680.
10. Murakami, K., Mihara, K. & Omura, T. (1994) J. Biochem. (Tokyo) 116, 164-175.
11. Szczesnaskorupa, E., Ahn, K. S., Chen, C. D., Doray, B. & Kemper, B. (1995) J. Biol. Chem. 270, 24327-24333.
12. Jackson, M. R., Cohendoyle, M. F., Peterson, P. A. & Williams, D. B. (1994) Science 263, 384-387.
13. Rajagopalan, S., Xu, Y. H. & Brenner, M. B. (1994) Science 263, 387-390.
14. Tolchinsky, S., Yuk, M. H., Ayalon, M., Lodish, H. F. & Lederkremer, G. Z. (1996) J. Biol. Chem. 271, 14496-14503.
15. Lederkremer, G. Z. & Lodish, H. F. (1991) J. Biol. Chem. 266, 1237-1244.
16. Spiess, M., Schwartz, A. L. & Lodish, H. F. (1985) J. Biol. Chem. 260, 1979-1982.
17. Landt, O., Grunert, H. P. & Hahn, U. (1990) Gene 96, 125-128.
18. Martin-Zanca, D., Oskam, R., Mitra, G., Copeland, T. & Barbacid, M. (1989) Mol. Cell. Biol. 9, 24-33.
19. Chen, C. A. & Okayama, H. (1988) BioTechniques 6, 632-638.
20. Louvard, D., Reggio, H. & Warren, G. (1982) J. Cell Biol. 92, 92-107.
21. Saraste, J. & Svensson, K. (1991) J. Cell Sci. 100, 415-430.
22. Hebert, D. N., Foellmer, B. & Helenius, A. (1995) Cell 81, 425-433.
23. Ou, W. J., Cameron, P. H., Thomas, D. Y. & Bergeron, J. J. M. (1993) Nature (London) 364, 771-776.
24. Braakman, I., Helenius, J. & Helenius, A. (1992) Nature (London) 356, 260-262.
25. Lodish, H. F., Kong, N. & Wikstrom, L. (1992) J. Biol. Chem. 267, 12753-12760.
26. Spiess, M. (1990) Biochemistry 29, 1009-1018.
27. Bischoff, J. & Lodish, H. F. (1987) J. Biol. Chem. 262, 11825-11832.
28. Pelham, H. R. B. (1995) Curr. Opin. Cell Biol. 7, 530-535.
29. Kornfeld, R. & Kornfeld, S. (1985) Annu. Rev. Biochem. 54, 631-664.
30. Tai, T., Yamashita, K., Ogata, A. M., Koide, N. & Muramatsu, T. (1975) J. Biol. Chem. 250, 8569-8575.
31. Wikstrom, L. & Lodish, H. F. (1991) J. Cell Biol. 113, 997-1007.
32. Bause, E., Breuer, W., Schweden, J., Roeser, R. & Geyer, R. (1992) Eur. J. Biochem. 208, 451-457.
33. Bischoff, J. & Kornfeld, R. (1986) J. Biol. Chem. 261, 4758-4765.
34. Cole, N. B., Sciaky, N., Marotta, A., Song, J. & Lippincottschwartz, J. (1996) Mol. Biol. Cell 7, 631-650.
35. Scherer, P. E., Lederkremer, G. Z., Williams, S., Fogliano, M., Baldini, G. & Lodish, H. F. (1996) J. Cell Biol. 133, 257-268.
36. Neumann, D., Yuk, M. H., Lodish, H. F. & Lederkremer, Z. (1996) Biochem. J. 313, 391-399.
37. Bonifacino, J. S., Cosson, P., Shah, N. & Klausner, R. D. (1991) EMBO J. 10, 2783-2793.
38. Yuk, M. H. & Lodish, H. F. (1993) J. Cell Biol. 123, 1735-1749.
39. Alberini, C. M., Bet, P., Milstein, C. & Sitia, R. (1990) Nature (London) 347, 485-487.
40. Blount, P. & Merlie, J. P. (1988) J. Biol. Chem. 263, 1072-1080.
41. Field, M. C., Moran, P., Li, W., Keller, G. A. & Caras, I. W. (1994) J. Biol. Chem. 269, 10830-10837.
42. Liu, Y., Choudhury, P., Cabral, C. M. & Sifers, R. N. (1997) J. Biol. Chem. 272, 7946-7951.
43. Teckman, J. H. & Perlmutter, D. H. (1996) J. Biol. Chem. 271, 13215-13220.
44. Hauri, H. P. & Schweizer, A. (1992) Curr. Opin. Cell Biol. 4, 600-608.
45. Hammond, C. & Helenius, A. (1994) J. Cell Biol. 126, 41-52.
46. Raposo, G., Vansanten, H. M., Leijendekker, R., Geuze, H. J. & Ploegh, H. L. (1995) J. Cell Biol. 131, 1403-1419.
47. Hsu, V. W., Yuan, L. C., Nuchtern, J. G., Lippincott, S. J., Hammerling, G. J. & Klausner, R. D. (1991) Nature (London) 352, 441-444.
48. Isidoro, C., Maggioni, C., Demoz, M., Fra, A. M. & Sitia, R. (1996) J. Biol. Chem. 271, 26138-26142.
49. Sonnichsen, B., Fullekrug, J., Van, P. N., Diekmann, W., Robinson, D. G. & Mieskes, G. (1994) J. Cell Sci. 107, 2705-2717.