The endoplasmic reticulum: Integration of protein folding, quality control, signaling and degradation

Current Opinion in Structural Biology

Volumn 11, Issue 1, 2001, Pages 120-124

  Chevet, Eric ^a   Cameron, Pamela H ^a   Pelletier, Marc F ^a   Thomas, David Y ^a   Bergeron, John J M ^a  

^a MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CALRETICULIN; GLUCOSE REGULATED PROTEIN; ISOMERASE; PROTEIN DISULFIDE ISOMERASE; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); SECRETORY PROTEIN;

CATALYSIS; CELL FUNCTION; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECRETION; PROTEIN TRANSPORT; QUALITY CONTROL; REVIEW;

EID: 0035253122     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00168-8     Document Type: Review

References (47)

1. Expression of a gene for cyclophilin which contains an amino-terminal endoplasmic reticulum-targeting signal
2. Protein folding in a specialized compartment: The endoplasmic reticulum
3. Role and regulation of the ER chaperone BiP
4. The glucose-regulated proteins (GRP78 and GRP94): Functions, gene regulation, and applications
5. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin
6. Calnexin family members as modulators of genetic diseases
7. Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum
8. Glycoprotein folding in the endoplasmic reticulum: A tale of three chaperones?
9. Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation
10. Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme
11. Structure and folding of nascent polypeptide chains during protein translocation in the endoplasmic reticulum
12. Unfolded protein response-induced BiP/Kar2p production protects cell growth against accumulation of misfolded protein aggregates in the yeast endoplasmic reticulum
13. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
14. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
15. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
16. Identification of a novel mechanism for the removal of glucose residues from high mannose-type oligosaccharides
17. Setting the standards: Quality control in the secretory pathway
18. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
19. Processing by endoplasmic reticulum mannosidases partitions a secretion-impaired glycoprotein into distinct disposal pathways
20. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
21. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
22. Cloning of mammalian Ire1 reveals diversity in the ER stress responses
23. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
24. A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response
25. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
26. Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
27. Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response
28. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
29. Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress
30. Perk is essential for translational regulation and cell survival during the unfolded protein response
31. A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B
32. Activation of transcription factor NF-kappaB by the adenovirus E3/19K protein requires its ER retention
33. 2+ and reactive oxygen intermediates as messengers
34. Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome
35. Retrograde protein translocation: ERADication of secretory proteins in health and disease
36. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
37. Role of Cue1p in ubiquitination and degradation at the ER surface
38. Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes
39. Molecular chaperone systems in the endoplasmic reticulum
40. Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin
41. Glucosidase and mannosidase inhibitors mediate increased secretion of mutant alpha1 antitrypsin Z
42. Oligosaccharide trimming plays a role in the endoplasmic reticulum-associated degradation of tyrosinase
43. The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome
44. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
45. The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control
46. Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway
47. A regulatory link between ER-associated protein degradation and the unfolded-protein response