The glycosylation and orientation in the membrane of the third cytoplasmic loop of human P-glycoprotein is affected by mutations and substrates

Biochemistry

Volumn 38, Issue 16, 1999, Pages 5124-5129

  Loo, Tip W ^a   Clarke, David M ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; GLYCOPROTEIN P;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; GLYCOSYLATION; HUMAN; HUMAN CELL; POINT MUTATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ADENOSINE TRIPHOSPHATASES; CELL LINE; CELL MEMBRANE; ENZYME ACTIVATION; GLYCOSYLATION; HUMANS; KIDNEY; MUTAGENESIS, SITE-DIRECTED; P-GLYCOPROTEIN; PEPTIDE FRAGMENTS; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY; VERAPAMIL;

EID: 0033586789     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982525y     Document Type: Article

References (34)

1. Bosch, I., and Croop, J. (1996) Biochim. Biophys. Acta 1288 (2), F37-F54.
2. Kim, R. B., Fromm, M. F., Wandel, C., Leake, B., Wood, A. J., Roden, D. M., and Wilkinson, G. R. (1998) J. Clin. Invest. 101 (2), 289-294.
3. Chen, C. J., Chin, J. E., Ueda, K., Clark, D. P., Pastan, I., Gottesman, M. M., and Roninson, I. B. (1986) Cell 47 (3), 381-389.
4. Higgins, C. F. (1992) Annu Rev. Cell Biol 8, 67-113.
5. Loo, T. W., and Clarke, D. M. (1994) J. Biol. Chem. 269 (10), 7243-7248.
6. Loo, T. W., and Clarke, D. M. (1997) J. Biol. Chem. 272 (2), 709-712.
7. Zhang, J. T., and Ling, V. (1991) J. Biol. Chem. 266 (27), 18224-18232.
8. Zhang, J. T., Duthie, M., and Ling, V. (1993) J. Biol. Chem. 268 (20), 15101-15110.
9. Zhang, M., Wang, G., Shapiro, A., and Zhang, J. T. (1996) Biochemistry 35 (30), 9728-9736.
10. Skach, W. R., Calayag, M. C., and Lingappa, V. R. (1993) J. Biol. Chem. 268 (10), 6903-6908.
11. Loo, T. W., and Clarke, D. M. (1994) J. Biol. Chem. 269 (46), 28683-28689.
12. Loo, T. W., and Clarke, D. M. ( 1995) J. Biol. Chem. 270 (37), 21839-21844.
13. Loo, T. W., and Clarke, D. M. (1998) J. Biol. Chem. 273 (24), 14671-14674.
14. Loo, T. W., and Clarke, D. M. (1995) J. Biol. Chem. 270 (2), 843-848.
15. Kast, C., Canfield, V., Levenson, R., and Gros, P. (1995) Biochemistry 34 (13), 4402-4411.
16. Kast, C., Canfield, V., Levenson, R., and Gros, P. (1996) J. Biol. Chem. 271 (16), 9240-9248.
17. Loo, T. W., and Clarke, D. M. (1994) J. Biol. Chem. 269 (10), 7750-7755.
18. Loo, T. W., and Clarke, D. M. (1996) J. Biol. Chem. 271 (44), 27488-27492.
19. Loo, T. W., and Clarke, D. M. (1993) J. Biol. Chem. 268 (5), 3143-3149.
20. Loo, T. W., and Clarke, D. M. (1995) J. Biol. Chem. 270 (37), 21449-21452.
21. Kornfeld, R., and Kornfeld, S. (1985) Annu Rev. Biochem. 54, 631-664.
22. Zhang, J. T., and Ling, V. (1993) Biochim. Biophys. Acta 1153 (2), 191-202.
23. Seibert, F. S., Linsdell, P., Loo, T. W., Hanrahan, J. W., Clarke, D. M., and Riordan, J. R. (1996) J. Biol. Chem. 271 (25), 15139-15145.
24. Ambudkar, S. V., Cardarelli, C. O., Pashinsky, I., and Stein, W. D. (1997) J. Biol. Chem. 272 (34), 21160-21166.
25. Hartmann, E., Rapoport, T. A., and Lodish, H. F. (1989) Proc. Natl. Acad. Sci. U.S.A. 86 (15), 5786-5790.
26. von Heijne, G. (1996) Prog. Biophys. Mol. Biol. 66 (2), 113-139.
27. von Heijne, G. (1997) Mol. Microbiol. 24 (2), 249-253.
28. Sato, M., Hresko, R., and Mueckler, M. (1998) J. Biol. Chem. 273 (39), 25203-25208.
29. Sipos, L., and von Heijne, G. (1993) Eur. J. Biochem. 213 (3), 1333-1340.
30. Denzer, A. J., Nabholz, C. E., and Spiess, M. (1995) EMBO J. 14 (24), 6311-6317.
31. Wahlberg, J. M., and Spiess, M. (1997) J. Cell Biol. 137 (3), 555-562.
32. van Klompenburg, W., Nilsson, I., von Heijne, G., and de Kruijff, B. (1997) EMBO J. 16 (14), 4261-4266.
33. Han, E. S., and Zhang, J. T. (1998) Biochemistry 37 (34), 11996-12004.
34. Ostedgaard, L. S., Rich, D. P., DeBerg, L. G., and Welsh, M. J. (1997) Biochemistry 36 (6), 1287-1294.