• 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. Objectives
3. Role of quality control in cell processes
4. Eukaryotic cells are highly compartmentalized
5. The ER environment
6. ER protein folding and quality control
7. Protein folding: ribonuclease A
8. Molecular chaperones
9. Protein disulfide isomerase (PDI)
10. PDIs which are present in the lumen
11. Prolyl cis-trans isomerase (PPI)
12. Molecular chaperones and foldases in the ER
13. N-glycosylation
14. N-glycan precursor synthesis
15. Glc3Man9GlcNAc2 glycan trimming in the ER
16. Calnexin: a lectin type chaperone
17. Calnexin transiently interacts with glycoproteins
18. The calnexin cycle (1)
19. Calnexin binds monoglucosylated glycoproteins
20. Binding of Glc1Man9 RNaseB intermediates
21. Calnexin lumenal domain
22. The calnexin cycle (2)
23. ERp57
24. RNase B refolding, catalyzed by ERp57 or PDI (1)
25. RNase B refolding, catalyzed by ERp57 or PDI (2)
26. Mapping the ERp57 binding site on calnexin
27. ERp57 structure and the calnexin binding site
28. PPIs also interact with calnexin/calreticulin
29. PDI-bb' domains can bind hydrophobic peptides
30. UDP-glucose glucosyl glycoprotein transferase
31. Man9GlcNAc2 glycoproteins from yeast DT111
32. Glucosylation of Man9GlcNAc2 glycopeptides
33. Rank order of peptides glucosylated by UGGT
34. Structure of beta-glucanase
35. UGGT substrates can be mutant but active
36. The calnexin cycle (3)
37. Disposal of misfolded glycoproteins by ERAD
38. The fate of glycoproteins
39. The ER quality control apparatus
40. ER quality control
41. Concluding words

Topics Covered

• The endoplasmic reticulum
• Protein folding
• Molecular chaperones
• N-glycosylation
• Lectin-type chaperones calnexin and calreticulin
• Link between protein folding and glycosylation
• ER quality control

Links

Series:

• Protein Homeostasis

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Publication History

• Published on February 2, 2012

Financial Disclosures

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