From the cradle to the grave: Molecular chaperones that may choose between folding and degradation

EMBO Reports

Volumn 2, Issue 10, 2001, Pages 885-890

  Höhfeld, Jörg ^a   Cyr, Douglas M ^b   Patterson, Cam ^c  

^a UNIVERSITY OF BONN   (Germany)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEINASE;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENERGY; EUKARYOTE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN QUALITY; REGULATORY MECHANISM;

ANIMALS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; LIGASES; MODELS, BIOLOGICAL; MODELS, GENETIC; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; UBIQUITIN;

EUKARYOTA;

EID: 0034756104     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kve206     Document Type: Article

References (41)

1. The U box is a modified RING finger - A common domain in ubiquitylation
2. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
3. The proteasome: A paradigm of a self-compartmentalizing protease
4. Stress management - Heat shock protein-70 and the regulation of apoptosis
5. Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70
6. Hsp90 & co. - A holding for folding
7. The Hsp70 and Hsp60 chaperone machines
8. Hsp90's secrets unfold: New insights from structural and functional studies
9. Regulation of heat shock protein-mediated protein triage decisions by the co-chaperone CHIP
10. The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors
11. Cooperation of an ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
12. Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains
13. Chaperones get in touch: The Hip-Hop connection
14. Molecular chaperones in protein folding
15. U-box proteins as a new family of ubiquitin-protein ligases
16. GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1
17. The lore of the RINGs: Substrate recognition and catalysis by ubiquitin ligases
18. Ubiquitin and its kin: How close are the family ties?
19. CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
20. A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch
21. The hPLIC proteins may provide a link between the ubiquitylation machinery and the proteasome
22. A novel ubiquitylation factor, E4, is involved in multiubiquitin chain assembly
23. Biosynthesis and degradation of CFTR
24. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
25. Cofactor-induced modulation of the functional specificity of the molecular chaperone Hsc70
26. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
27. p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: Suppression by BAG-1
28. The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
29. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
30. Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90
31. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
32. Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
33. Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90
34. Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
35. Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth
36. Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activity
37. Reversible inhibition of Hsp70 chaperone function by Sythe and Reaper
38. The ubiquitin system
39. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
40. Posttranslational quality control: Folding, refolding, and degrading proteins
41. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23