Peripheral protein quality control removes unfolded CFTR from the plasma membrane

Science

Volumn 329, Issue 5993, 2010, Pages 805-810

  Okiyoneda, Tsukasa ^a   Barrière, Hervé ^a   Bagdány, Miklós ^a   Rabeh, Wael M ^a   Du, Kai ^a   Höhfeld, Jörg ^b   Young, Jason C ^a   Lukacs, Gergely L ^a  

^a MCGILL UNIVERSITY   (Canada)

^b UNIVERSITY OF BONN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PROTEIN; SMALL INTERFERING RNA; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE;

CONDUCTIVITY; ENVIRONMENTAL STRESS; ENZYME; GENETIC ANALYSIS; HOMEOSTASIS; MEMBRANE; PLASMA; PROTEIN; QUALITY CONTROL;

ARTICLE; CELL MEMBRANE; CELL SURFACE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; ENVIRONMENTAL STRESS; HOMEOSTASIS; HUMAN; HUMAN CELL; LYSOSOME; PERIPHERAL PROTEIN QUALITY CONTROL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROCESSING; QUALITY CONTROL; UBIQUITINATION;

CELL MEMBRANE; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; GLYCOSYLATION; HELA CELLS; HOMEOSTASIS; HSC70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; LYSOSOMES; MOLECULAR CHAPERONES; MUTANT PROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TRANSPORT; RECOMBINANT PROTEINS; RNA, SMALL INTERFERING; TEMPERATURE; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATED PROTEINS; UBIQUITINATION;

EID: 77955607650     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1191542     Document Type: Article

References (41)

1. T. Anelli, R. Sitia, EMBO J. 27, 315 (2008).
2. D. N. Hebert, M. Molinari, Physiol. Rev. 87, 1377 (2007).
3. E. T. Powers, R. I. Morimoto, A. Dillin, J. W. Kelly, W. E. Balch, Annu. Rev. Biochem. 78, 959 (2009).
4. S. S. Vembar, J. L. Brodsky, Nat. Rev. Mol. Cell Biol. 9, 944 (2008).
5. M. Sharma et al., J. Cell Biol. 164, 923 (2004).
6. R. Glozman et al., J. Cell Biol. 184, 847 (2009).
7. H. Hayashi, Y. Sugiyama, Mol. Pharmacol. 75, 143 (2009).
8. S. Dupré, D. Urban-Grimal, R. Haguenauer-Tsapis, Biochim. Biophys. Acta 1695, 89 (2004).
9. J. H. Hurley, S. D. Emr, Annu. Rev. Biophys. Biomol. Struct. 35, 277 (2006).
10. P. Arvan, X. Zhao, J. Ramos-Castaneda, A. Chang, Traffic 3, 771 (2002).
11. S. Alberti, K. Böhse, V. Arndt, A. Schmitz, J. Höhfeld, Mol. Biol. Cell 15, 4003 (2004).
12. G. C. Meacham, C. Patterson, W. Zhang, J. M. Younger, D. M. Cyr, Nat. Cell Biol. 3, 100 (2001).
13. J. M. Younger et al., Cell 126, 571 (2006).
14. D. Morito et al., Mol. Biol. Cell 19, 1328 (2008).
15. G. M. Denning et al., Nature 358, 761 (1992).
16. J. M. Younger et al., J. Cell Biol. 167, 1075 (2004).
17. D. E. Grove, M. F. Rosser, H. Y. Ren, A. P. Naren, D. M. Cyr, Mol. Biol. Cell 20, 4059 (2009).
18. N. Pedemonte et al., J. Clin. Invest. 115, 2564 (2005).
19. Materials and methods are available as supporting material on Science Online.
20. K. Du, M. Sharma, G. L. Lukacs, Nat. Struct. Mol. Biol. 12, 17 (2005).
21. M. Sharma, M. Benharouga, W. Hu, G. L. Lukacs, J. Biol. Chem. 276, 8942 (2001).
22. H. Barriere et al., Traffic 7, 282 (2006).
23. O. Staub, D. Rotin, Physiol. Rev. 86, 669 (2006).
24. X. Wang et al., Cell 127, 803 (2006).
25. Single-letter abbreviations for the amino acid residues used in this article are as follows: A, Ala; H, His; K, Lys; and Q, Gln.
26. C. A. Ballinger et al., Mol. Cell. Biol. 19, 4535 (1999).
27. S. B. Goldfarb et al., Proc. Natl. Acad. Sci. U.S.A. 103, 5817 (2006).
28. W. Xu et al., Proc. Natl. Acad. Sci. U.S.A. 99, 12847 (2002).
29. S. Murata, Y. Minami, M. Minami, T. Chiba, K. Tanaka, EMBO Rep. 2, 1133 (2001).
30. V. Arndt, C. Rogon, J. Höhfeld, Cell. Mol. Life Sci. 64, 2525 (2007).
31. Y. Minami, J. Höhfeld, K. Ohtsuka, F. U. Hartl, J. Biol. Chem. 271, 19617 (1996).
32. S. Tzankov, M. J. Wong, K. Shi, C. Nassif, J. C. Young, J. Biol. Chem. 283, 27100 (2008).
33. T. Okiyoneda et al., Mol. Biol. Cell 15, 563 (2004).
34. K. Harada et al., J. Biol. Chem. 281, 12841 (2006).
35. M. A. Loo et al., EMBO J. 17, 6879 (1998).
36. G. C. Meacham et al., EMBO J. 18, 1492 (1999).
37. M. Zhang et al., Mol. Cell 20, 525 (2005).
38. D. Finley, Annu. Rev. Biochem. 78, 477 (2009).
39. B. K. Sato, D. Schulz, P. H. Do, R. Y. Hampton, Mol. Cell 34, 212 (2009).
40. J. M. Bomberger, R. L. Barnaby, B. A. Stanton, J. Biol. Chem. 284, 18778 (2009).
41. 10 cells, respectively; H. Stenmark for Hrs antibody; and H. Lewis, C. Lima, and K. Iwai for NBD1-3S, SUMO, Ulp1, and UbcH5 plasmids, respectively. Lamp1, Lamp2, and CD63 antibodies were developed by J. August and J. Hildreth (University of Iowa). T.O. and W.M.R. were supported by a Canadian Cystic Fibrosis Foundation and a Groupe de Recherche Axé sur la Structure des Protéines (GRASP) postdoctoral fellowship, respectively. This work was supported by grants to J.H. from Deutsche Forschungsgemeinschaft, J.C.Y. and G.L.L. from the Canadian Institute of Health Resources, NIH, Cystic Fibrosis Foundation Therapeutics, the Canadian Cystic Fibrosis Foundation, and the Canadian Foundation for Innovation. J.C.Y. and G.L.L. are holders of Canada Research Chairs.