• Overview of Chaperone Networks
• 41 min
  1. Mapping the molecular chaperone interaction network in yeast

  • Prof. Walid A. Houry
• 30 min
  2. The interaction network of the GroEL chaperonin

  • Prof. Dr. F. Ulrich Hartl
• 61 min
  3. Human heat shock protein families

  • Prof. Herman Kampinga
• 42 min
  4. Extracellular proteostasis: an emerging field

  • Prof. Mark Wilson
• 36 min
  5. Protein homeostasis and the chaperone interaction network in Arabidopsis thaliana

  • Prof. Rongmin Zhao
• Proteasome Networks
• 64 min
  6. Biogenesis of the eukaryotic proteasome

  • Prof. Mark Hochstrasser
• Understanding Intrinsically Disordered Proteins in Protein Homeostasis
• 36 min
  7. Intrinsically unstructured proteins: regulation and disease

  • Dr. M. Madan Babu
• 43 min
  8. The roles of intrinsic disorder in protein interaction networks

  • Prof. Vladimir N. Uversky
• Gene Regulatory Networks and their Role in Protein Homeostasis
• 38 min
  9. Network motifs: basic building blocks of biological networks

  • Prof. Uri Alon
• 41 min
  10. Structure, evolution and dynamics of gene regulatory networks

  • Dr. M. Madan Babu
• 33 min
  11. Computational methods in analysis of gene regulation and protein interactions

  • Prof. Ron Shamir
• 51 min
  12. Protein-protein interaction networks

  • Prof. Peter Csermely
• Protein Homeostasis in the Endoplasmic Reticulum
• 56 min
  13. Role of calnexin and calreticulin in protein homeostasis within the endoplasmic reticulum

  • Prof. David B. Williams
• 30 min
  14. The unfolded protein response

  • Prof. Kazutoshi Mori
• 38 min
  15. Role of ER stress in cystic fibrosis airway inflammation

  • Dr. Carla Maria Pedrosa Ribeiro
• 57 min
  16. The recognition of misfolded glycoproteins in the endoplasmic reticulum

  • Dr. David Y. Thomas
• 49 min
  17. Chaperone systems of the endoplasmic reticulum

  • Prof. Linda M. Hendershot
• 74 min
  18. The ERAD network

  • Prof. Daniel Hebert
• Protein Homeostasis in the Mitochondria
• 22 min
  19. Protein homeostasis in mitochondria: AAA+ chaperones & proteases

  • Dr. David A. Dougan
• 46 min
  20. Protein homeostasis in mitochondria: chaperones and proteases of the mitochondrial matrix

  • Prof. Wolfgang Voos
• 26 min
  21. Mitochondrial chaperonin Hsp60: locations, functions and pathology

  • Prof. Francesco Cappello
  • Prof. Alberto J. L. Macario
• Protein Homeostasis in the Nucleus
• 23 min
  22. Nuclear protein quality control degradation

  • Dr. Richard G. Gardner
• Protein Homeostasis in Aging Disease
• 27 min
  23. Protein homeostasis during ageing: C. elegans as a model organism

  • Prof. Nektarios Tavernarakis
• Protein Homeostasis in Neurodegeneration
• 41 min
  24. Endoplasmic reticulum stress in neurodegenerative diseases

  • Prof. Claudio Soto
• 48 min
  25. Roles for Hsp40 molecular chaperones in protein misfolding disease

  • Prof. Douglas M. Cyr
• 38 min
  26. Protein folding in vivo

  • Prof. James Bardwell
• 39 min
  27. Protein degradation and defense against neurodegenerative disease 1

  • Prof. Alfred Goldberg
• 42 min
  28. Protein degradation and defense against neurodegenerative disease 2

  • Prof. Alfred Goldberg

Printable Handouts

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Navigable Slide Index

1. Introduction
2. Protein folding in vitro
3. Protein folding in vivo
4. Interests
5. Chaperones
6. HdeA protects E. coli from stomach acid
7. E. coli under non-stress conditions
8. HdeA mechanism
9. FRET to monitor HdeA conformation
10. HdeA unfolding monitored by FRET
11. HdeA adaptively binds substrates
12. HdeA releases substrates very slowly
13. Monitoring structural changes in HdeA
14. Examine HdeA
15. Examine substrate
16. In vivo folding
17. Ways to measure folding and stability
18. To better understand in vivo folding
19. A tripartite fusion system
20. Quantitative in vivo stability readout
21. Proteins inserted into beta-lactamase
22. Selection for stabilized IM7 variants
23. PenV-resistant IM7 mutants are stabilized
24. Most proteins are only marginally stable
25. Why are proteins so unstable?
26. Stabilizing mutations map to binding interface
27. Optimizing folding in vivo
28. A dual selection system
29. Effect instability of the inserted protein
30. Fold or die!
31. IM7 and Spy in the periplasm of EMS strains
32. BaeS regulates Spy
33. Spy overproduction is sufficient to stabilize IM7
34. Spy inhibits MDH aggregation
35. Spy suppresses protein aggregation
36. Spy enhances protein refolding
37. Spy and tannins
38. Spy forms a thin cradle shaped dimer
39. Substrate binding and environment changes
40. Optimization of in vivo folding
41. Acknowledgments

Topics Covered

• Protein folding in vivo
• Protein folding as facilitated by the acid inducible chaperone HdeA
• Optimization of folding in vivo illustrates a tradeoff between stability and function
• The Spy chaperone

Links

Series:

• Protein Homeostasis

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Publication History

• Published on February 2, 2012

Financial Disclosures

• Prof. James Bardwell has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.