• Overview of Molecular Chaperones
• 34 min
  1. History of the molecular chaperone concept: roles in assembly processes

  • Prof. Emeritus R. John Ellis
• 34 min
  2. Chaperone mechanisms in cellular protein folding

  • Prof. Dr. F. Ulrich Hartl
• Prokaryotic Molecular Chaperones
• 38 min
  3. Mechanistic aspects of chaperonin GroEL/ES function

  • Prof. Amnon Horovitz
• 99 min
  4. Structure and function of the ATP-dependent Clp chaperone/protease machines

  • Dr. Michael R. Maurizi
• 32 min
  5. The role of chaperones and Sec machinery in protein secretion

  • Prof. Koreaki Ito
• 44 min
  6. How can molecular chaperones repair damaged protein structures?

  • Prof. Pierre Goloubinoff
• 32 min
  7. Disulfide bond formation in vivo

  • Prof. James Bardwell
• Eukaryotic Molecular Chaperones
• 39 min
  8. Overview of eukaryotic molecular chaperones in the cytosol

  • Dr. Jason C. Young
• 36 min
  9. Chaperonin-containing TCP-1 (CCT), actin springs, and protein folding fluxes

  • Prof. Keith Willison
• 35 min
  10. The functions of the Hsp70 system

  • Prof. Jeffrey L. Brodsky
• 26 min
  11. Hsp90: a chaperone for protein kinases and hormone receptors

  • Dr. David Toft
• Role of Chaperones in Diseases
• 38 min
  12. The roles of molecular chaperones in bacterial infection

  • Prof. Tomoko Yamamoto
• 46 min
  13. Role of chaperonin-like proteins in Bardet-Biedl syndrome

  • Dr. Michel R. Leroux
• 53 min
  14. Roles for molecular chaperones in cystic fibrosis

  • Prof. Douglas M. Cyr
• 51 min
  15. Targeting cancer: designing drugs against Hsp90

  • Dr. Gabriela Chiosis
• Archived Lectures *These may not cover the latest advances in the field
• 29 min
  16. Overview of prokaryotic molecular chaperones

  • Prof. Walid A. Houry
• 47 min
  17. The biogenesis of E. coli inner membrane proteins

  • Dr. Joen Luirink
• 39 min
  18. Mechanism of chaperone action of small heat shock proteins

  • Prof. Elizabeth Vierling
• 22 min
  19. ClpB: a chaperone for protein disaggregation

  • Prof. Michal Zolkiewski
• 38 min
  20. The roles of chaperonins in bacteria

  • Dr. Peter Lund
• 44 min
  21. Towards a unifying mechanism for the Hsp70 chaperones

  • Prof. Pierre Goloubinoff
• 29 min
  22. Adaptor mediated activation of the Hsp100/ Clp protein ClpC controls general and regulatory proteolysis in Bacillus subtilis

  • Prof. Dr. Kursad Turgay
• 33 min
  23. Hsp31: a general stress protein of Escherichia coli

  • Prof. Francois Baneyx
• 46 min
  24. Hsp104: a specialized chaperone for protein disaggregation

  • Dr. John R. Glover
• 47 min
  25. Molecular chaperones and handling of abnormal proteins in neurodegenerative disorders

  • Prof. Michael Sherman
• 20 min
  26. The role of chaperones in Parkinson's disease

  • Dr. Konstanze F. Winklhofer

Printable Handouts

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Navigable Slide Index

1. Introduction
2. Talk outline
3. Hsp90
4. Molecular chaperones
5. Early studies on Hsp90/client interaction
6. Hsp90 client proteins
7. Hsp90 clients
8. Hsp90 biology
9. Chaperoning steroid receptors
10. Steroid receptor action
11. The assembly of Hsp90 complexes with PR
12. PR chaperoning cycle
13. The Hsp90 machine
14. In vitro approaches
15. 5-protein system
16. Time course of PR complex assembly
17. Loading Hsp90 and conformational change
18. Intermediate complex assembly
19. Steps promoting conformational change
20. Hsp90 structure
21. Conformational states
22. Hsp90 domains
23. Hsp90 domains - N terminal domain
24. A model of N domain with bound ADP
25. Hsp90 inhibitors
26. Hsp90 domains - M domain
27. Hsp90 domains - C terminal domain
28. E. coli Hsp90 in open conformation (1)
29. E. coli Hsp90 in open conformation (2)
30. Yeast Hsp90 in ATP-bound conformation (1)
31. Yeast Hsp90 in ATP-bound conformation (2)
32. Hsp90 structure: in the absence of ATP
33. Hsp90 structure: ATP-bound state
34. Hsp90 structure: additional conformational states
35. Do various clients have specific needs?
36. Checkpoint kinase 1 (Chk1)
37. 5-protein system: Cdc37 and CK3
38. Chk1 kinase activity
39. Chk1 vs. PR
40. Alternate pathways for different clients
41. Co-chaperones provide diversity to Hsp90
42. Hsp90 co-chaperones
43. Role of co-chaperones
44. Coordinating conformation and function of Hsp90
45. Recognizing specific client groups
46. Bringing an additional activity to Hsp90 complexes
47. Trafficking or other specialized functions
48. Co-chaperones are targets for inhibitor drugs
49. Co-chaperone binding
50. Mouse knockout studies
51. Some key questions
52. What is the big picture?
53. End of the talk
54. Bibliography (1)
55. Bibliography (2)
56. Bibliography (3)
57. Websites

Topics Covered

• Chaperoning steroid receptors; the Hsp90 chaperoning machine
• Hsp90 structure and function
• Chaperoning protein kinases and other Hsp90 clients

Links

Series:

• Molecular Chaperones

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Publication History

• Published on October 1, 2007

Financial Disclosures

• Dr. David Toft has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.