Futile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway

Science

Volumn 340, Issue 6135, 2013, Pages 978-981

  Xu, Chengchao ^a   Wang, Songyu ^a,b   Thibault, Guillaume ^a   Ng, Davis T W ^a,b,c  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b DUKE NUS MEDICAL SCHOOL   (Singapore)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

REACTIVE OXYGEN METABOLITE;

DEGRADATION; ENERGY EFFICIENCY; MOLECULAR ANALYSIS; PROTEIN; SUBSTRATE;

ARTICLE; CHEMICAL MODIFICATION; CITRIC ACID CYCLE; CYTOSOL; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; ENERGY RESOURCE; GLYCOSYLATION; HYDROPHILICITY; IN VITRO STUDY; MANNOSYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN REFOLDING; PROTEIN SYNTHESIS; PROTEIN UNFOLDING; STEADY STATE; UNFOLDED PROTEIN RESPONSE;

EID: 84877975094     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1234055     Document Type: Article

References (28)

1. F. U. Hartl, A. Bracher, M. Hayer-Hartl, Nature 475, 324 (2011).
2. J. S. Weissman, Y. Kashi, W. A. Fenton, A. L. Horwich, Cell 78, 693 (1994).
3. P. Määttänen, K. Gehring, J. J. Bergeron, D. Y. Thomas, Semin. Cell Dev. Biol. 21, 500 (2010).
4. K. Araki, K. Nagata, Cold Spring Harb. Perspect. Biol. 3, a007526 (2011).
5. M. C. Rodrigo-Brenni, R. S. Hegde, Dev. Cell 23, 896 (2012).
6. M. H. Smith, H. L. Ploegh, J. S. Weissman, Science 334, 1086 (2011).
7. D. E. Aronson, L. M. Costantini, E. L. Snapp, Traffic 12, 543 (2011).
8. R. Prasad, S. Kawaguchi, D. T. Ng, Mol. Biol. Cell 21, 2117 (2010).
9. A. Helenius, M. Aebi, Annu. Rev. Biochem. 73, 1019 (2004).
10. R. Gauss, K. Kanehara, P. Carvalho, D. T. Ng, M. Aebi, Mol. Cell 42, 782 (2011).
11. B. G. Reid, G. C. Flynn, Biochemistry 36, 6786 (1997).
12. A. C. Fisher, M. P. DeLisa, PLoS ONE 3, e2351 (2008).
13. E. M. Rubenstein, S. G. Kreft, W. Greenblatt, R. Swanson, M. Hochstrasser, J. Cell Biol. 197, 761 (2012).
14. C. Harty, S. Strahl, K. Römisch, Mol. Biol. Cell 12, 1093 (2001).
15. S. Vashist et al., J. Cell Biol. 155, 355 (2001).
16. K. Nakatsukasa et al., J. Biol. Chem. 279, 49762 (2004).
17. S. Li, R. A. Spooner, R. Y. Hampton, J. M. Lord, L. M. Roberts, PLoS ONE 7, e41119 (2012).
18. H. Hirayama, M. Fujita, T. Yoko-o, Y. Jigami, J. Biochem. 143, 555 (2008).
19. V. Goder, A. Melero, J. Cell Sci. 124, 144 (2011).
20. C. M. Coughlan, J. L. Walker, J. C. Cochran, K. D. Wittrup, J. L. Brodsky, J. Biol. Chem. 279, 15289 (2004).
21. M. Lommel, S. Strahl, Glycobiology 19, 816 (2009).
22. K. J. Travers et al., Cell 101, 249 (2000).
23. D. J. Sweet, H. R. Pelham, EMBO J. 11, 423 (1992).
24. F. Schwarz, M. Aebi, Curr. Opin. Struct. Biol. 21, 576 (2011).
25. M. C. Jonikas et al., Science 323, 1693 (2009).
26. J. S. Cox, P. Walter, Cell 87, 391 (1996).
27. S. Ghaemmaghami et al., Nature 425, 737 (2003).
28. G. Thibault, D. T. Ng, Cold Spring Harb. Perspect. Biol. 4, a013193 (2012).