• 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. CFTR protein and its mutations in CF patients
3. Mislocalization of deltaF508 CFTR
4. Consequences of defects in CFTR function
5. CFTR activity correlates with CF severity
6. Cystic fibrosis foundation therapeutics pipeline
7. CF and CFTR folding/degradation
8. Role of chaperones in CFTR biogenesis
9. Results of calnexin inactivation
10. Results of Hsc70 inactivation
11. Regulation of Hsp70 function by Hsp40
12. Type I Hsp40 proteins contain a CAAX box
13. Steps in the CFTR folding pathway
14. Does Hsc70 facilitate CFTR degradation?
15. U-box family
16. Results of CHIP overexpression
17. CHIP expression blocks CFTR processing
18. CHIP mediated triage of misfolded proteins
19. CFTR-deltaF508 partitioning between pathways
20. RMA1 is an ER localized RING E3
21. Elevation of Rma1 levels blocks CFTR folding
22. Results of Rma1 and Ubc6e reduction
23. E2/E3 ubiquitin ligase senses folded CFTR
24. Derlin-1 protein
25. Results of DER1 overexpression
26. Results of DER1 knockdown
27. Possible role of DER1
28. CFTR-deltaF508 sensitivity to Rma1 changes
29. Regions recognized by Rma1 and CHIP E3
30. Sensing delta-F508 folding defects
31. CFTR sub-domains recognition by Rma1/CHIP
32. Small molecules and CFTR folding efficiency
33. Results of treatment with VRT-532 and Corr4a
34. Recognition of CFTR-deltaF508 folding defects
35. Acknowledgements

Topics Covered

• Cystic fibrosis is a fatal homozygous recessive disorder
• Caused primarily by misfolding of mutant forms of cystic fibrosis transmembrane conductance regulator (CFTR)
• The folding defects in mutant CFTR are detected by protein quality control machines in the endoplasmic reticulum that target mutant CFTR for premature degradation
• Small molecules that are being developed as drugs to treat cystic fibrosis enable mutant CFTR to avoid recognition by the endoplasmic reticulum quality control system and function at the cell surface

Links

Series:

• Molecular Chaperones

Categories:

• Biochemistry
• Cell Biology
• Clinical Practice

Therapeutic Areas:

• Immunology & Inflammation
• Respiratory Diseases

Talk Citation

Publication History

• Published on October 1, 2007

Financial Disclosures

• Prof. Douglas M. Cyr has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.