Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1

FEBS Letters

Volumn 582, Issue 30, 2008, Pages 4143-4146

  Eisele, Frederik ^a   Wolf, Dieter H ^a  

^a UNIVERSITY OF STUTTGART   (Germany)

Author keywords

Misfolded protein; Proteasome; Protein degradation; Protein quality control; Ubiquitin ligase; Ubr1

Indexed keywords

CYTOPLASM PROTEIN; PROTEASOME; UBIQUITIN; UBIQUITIN LIGASE UBR1; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CYTOPLASM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; YEAST;

CYTOPLASM; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE DELETION; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

EID: 57049182407     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.11.015     Document Type: Article

References (32)

1. Sommer T., and Wolf D.H. Endoplasmic reticulum degradation: reverse protein flow of no return. Faseb J. 11 (1997) 1227-1233
2. Brodsky J.L., and McCracken A.A. ER protein quality control and proteasome-mediated protein degradation. Semin. Cell Dev. Biol. 10 (1999) 507-513
3. Kostova Z., and Wolf D.H. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J. 22 (2003) 2309-2317
4. Ellgaard L., Molinari M., and Helenius A. Setting the standards: quality control in the secretory pathway. Science 286 (1999) 1882-1888
5. Ellgaard L., and Helenius A. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4 (2003) 181-191
6. Raasi S., and Wolf D.H. Ubiquitin receptors and ERAD: a network of pathways to the proteasome. Semin. Cell Dev. Biol. 18 (2007) 780-791
7. Schäfer A., Kostova Z., and Wolf D.H. Endoplasmic reticulum protein quality control and degradation. In: Mayer R.J., Ciechanover A., and Rechsteiner M. (Eds). Protein Degradation (2008), Wiley-VCH Verlag, Weinheim 123-143
8. McClellan A.J., Scott M.D., and Frydman J. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 121 (2005) 739-748
9. Park S.H., Bolender N., Eisele F., Kostova Z., Takeuchi J., Coffino P., and Wolf D.H. The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system. Mol. Biol. Cell 18 (2007) 153-165
10. McClellan A.J., Tam S., Kaganovich D., and Frydman J. Protein quality control: chaperones culling corrupt conformations. Nat. Cell Biol. 7 (2005) 736-741
11. Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82 (2002) 373-428
12. Wolf D.H., and Hilt W. The proteasome: a proteolytic nanomachine of cell regulation and waste disposal. Biochim. Biophys. Acta 1695 (2004) 19-31
13. Biederer T., Volkwein C., and Sommer T. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15 (1996) 2069-2076
14. Hiller M.M., Finger A., Schweiger M., and Wolf D.H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273 (1996) 1725-1728
15. Esser C., Alberti S., and Höhfeld J. Cooperation of molecular chaperones with the ubiquitin-proteasome system. Biochim. Biophys. Acta 1695 (2004) 171-188
16. Sambrook J., Maniatis T., and Fritsch E.F.s. Molecular Cloning: A Laboratory Manual (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
17. Guthrie C., and Fink G.R.s. Guide to Yeast Genetics and Molecular and Cell Biology (2002), Academic Press, San Diego, California
18. Knop M., Hauser N., and Wolf D.H. N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12 (1996) 1229-1238
19. Gueldener U., Heinisch J., Koehler G.J., Voss D., and Hegemann J.H. A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast. Nucl. Acids Res. 30 (2002) e23
20. Kohlmann S., Schäfer A., and Wolf D.H. Ubiquitin ligase Hul5 is required for fragment-specific substrate degradation in endoplasmic reticulum-associated degradation. J. Biol. Chem. 283 (2008) 16374-16383
21. Du F., Navarro-Garcia F., Xia Z., Tasaki T., and Varshavsky A. Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain. Proc. Natl. Acad. Sci. USA 99 (2002) 14110-14115
22. Taxis C., Vogel F., and Wolf D.H. ER-golgi traffic is a prerequisite for efficient ER degradation. Mol. Biol. Cell 13 (2002) 1806-1818
23. Medicherla B., Kostova Z., Schaefer A., and Wolf D.H. A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Rep. 5 (2004) 692-697
24. Scheel, H. (2005) Comparative Analysis of the Ubiquitin-Proteasome System in Homo sapiens and Saccharomyces cerevisiae. Ph.D. Thesis, University of Cologne.
25. Buschhorn B.A., Kostova Z., Medicherla B., and Wolf D.H. A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. FEBS Lett. 577 (2004) 422-426
26. Schafer A., and Wolf D.H. Yeast genomics in the elucidation of endoplasmic reticulum (ER) quality control and associated protein degradation (ERQD). Methods Enzymol. 399 (2005) 459-468
27. Xia Z., Webster A., Du F., Piatkov K., Ghislain M., and Varshavsky A. Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway. J. Biol. Chem. 283 (2008) 24011-24028
28. Bartel B., Wunning I., and Varshavsky A. The recognition component of the N-end rule pathway. EMBO J. 9 (1990) 3179-3189
29. Xie Y., and Varshavsky A. The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain. EMBO J. 18 (1999) 6832-6844
30. Moerschell R.P., Hosokawa Y., Tsunasawa S., and Sherman F. The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation. J. Biol. Chem. 265 (1990) 19638-19643
31. Byrd C., Turner G.C., and Varshavsky A. The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor. EMBO J. 17 (1998) 269-277
32. Turner G.C., Du F., and Varshavsky A. Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway. Nature 405 (2000) 579-583