• 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

PDF

Navigable Slide Index

1. Introduction
2. The endoplasmic reticulum (ER)
3. ER is the first stage in the secretory pathway
4. Functions of the endoplasmic reticulum
5. Proteins involved in ER folding and quality control
6. Glycosylation and oligosaccharide processing
7. Glycoprotein recognition by Cnx/Crt
8. Cnx and Crt, glycoprotein-specific chaperones
9. Lectin-dependent binding to glycoproteins
10. Functions of calnexin and calreticulin
11. Cnx/Crt functions revealed by CAS treatment
12. Calnexin prevents aggregation
13. The "calnexin cycle"
14. UGGT - the folding "sensor" of the calnexin cycle
15. The observed functions of Cnx and Crt
16. Polypeptide-based interactions of Cnx/Crt
17. Polypeptide-based interactions in vitro
18. Characterization of the polypeptide binding site
19. Cnx and Crt possessing lectin & polypeptide sites
20. Cnx/Crt dual-binding model of glycoprotein
21. Two similar chaperones, differing substrates
22. Role of ERp57 in Cnx/Crt glycoprotein folding
23. ERp57 functions with calnexin and calreticulin
24. Interaction with a folding glycoprotein
25. Ternary complex of ERp57, calnexin and substrate
26. ERp57 receives most substrates from Cnx/Crt
27. ERp57 role in glycoprotein folding by Cnx/Crt
28. Peptidyl prolyl isomerases in the ER
29. Functions of peptidyl prolyl isomerases in the ER
30. Cyclophilin B interacts with Cnx/Crt
31. Model of glycoprotein folding
32. ER-associated degradation (ERAD)
33. Recognition of misfolded glycoproteins
34. The glyco code of the ER
35. Recruitment to the retrotranslocon
36. Summary

Topics Covered

• Introduction to the endoplasmic reticulum
• Protein folding and quality control within the endoplasmic reticulum
• Asn-linked glycosylation and oligosaccharide processing
• Calnexin and calreticulin
• Structure and functions
• The Calnexin cycle
• Recognition of substrate polypeptide by calnexin and calreticulin
• The dual binding model
• Role of ERp57 in glycoprotein folding by calnexin and calreticulin
• Peptidyl prolyl isomerases within the endoplasmic reticulum
• ER-associated degradation
• Overview
• Recognition of misfolded glycoproteins
• The Glyco code of the ER

Links

Series:

• Protein Homeostasis

Categories:

• Biochemistry
• Cell Biology

Talk Citation

Williams, D.B. (2012, February 2). Role of calnexin and calreticulin in protein homeostasis within the endoplasmic reticulum [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved March 21, 2025, from https://doi.org/10.69645/EBLK8893.
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Publication History

• Published on February 2, 2012

Financial Disclosures

• Prof. David B. Williams has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.