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- Overview of Chaperone Networks
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1. Mapping the molecular chaperone interaction network in yeast
- Prof. Walid A. Houry
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2. The interaction network of the GroEL chaperonin
- Prof. Dr. F. Ulrich Hartl
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3. Human heat shock protein families
- Prof. Herman Kampinga
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4. Extracellular proteostasis: an emerging field
- Prof. Mark Wilson
- Proteasome Networks
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6. Biogenesis of the eukaryotic proteasome
- Prof. Mark Hochstrasser
- Understanding Intrinsically Disordered Proteins in Protein Homeostasis
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7. Intrinsically unstructured proteins: regulation and disease
- Dr. M. Madan Babu
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8. The roles of intrinsic disorder in protein interaction networks
- Prof. Vladimir N. Uversky
- Gene Regulatory Networks and their Role in Protein Homeostasis
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10. Structure, evolution and dynamics of gene regulatory networks
- Dr. M. Madan Babu
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12. Protein-protein interaction networks
- Prof. Peter Csermely
- Protein Homeostasis in the Endoplasmic Reticulum
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13. Role of calnexin and calreticulin in protein homeostasis within the endoplasmic reticulum
- Prof. David B. Williams
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14. The unfolded protein response
- Prof. Kazutoshi Mori
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15. Role of ER stress in cystic fibrosis airway inflammation
- Dr. Carla Maria Pedrosa Ribeiro
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16. The recognition of misfolded glycoproteins in the endoplasmic reticulum
- Dr. David Y. Thomas
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17. Chaperone systems of the endoplasmic reticulum
- Prof. Linda M. Hendershot
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18. The ERAD network
- Prof. Daniel Hebert
- Protein Homeostasis in the Mitochondria
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19. Protein homeostasis in mitochondria: AAA+ chaperones & proteases
- Dr. David A. Dougan
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21. Mitochondrial chaperonin Hsp60: locations, functions and pathology
- Prof. Francesco Cappello
- Prof. Alberto J. L. Macario
- Protein Homeostasis in the Nucleus
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22. Nuclear protein quality control degradation
- Dr. Richard G. Gardner
- Protein Homeostasis in Aging Disease
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23. Protein homeostasis during ageing: C. elegans as a model organism
- Prof. Nektarios Tavernarakis
- Protein Homeostasis in Neurodegeneration
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24. Endoplasmic reticulum stress in neurodegenerative diseases
- Prof. Claudio Soto
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25. Roles for Hsp40 molecular chaperones in protein misfolding disease
- Prof. Douglas M. Cyr
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26. Protein folding in vivo
- Prof. James Bardwell
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27. Protein degradation and defense against neurodegenerative disease 1
- Prof. Alfred Goldberg
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28. Protein degradation and defense against neurodegenerative disease 2
- Prof. Alfred Goldberg
Printable Handouts
Navigable Slide Index
- Introduction
- The endoplasmic reticulum (ER)
- ER is the first stage in the secretory pathway
- Functions of the endoplasmic reticulum
- Proteins involved in ER folding and quality control
- Glycosylation and oligosaccharide processing
- Glycoprotein recognition by Cnx/Crt
- Cnx and Crt, glycoprotein-specific chaperones
- Lectin-dependent binding to glycoproteins
- Functions of calnexin and calreticulin
- Cnx/Crt functions revealed by CAS treatment
- Calnexin prevents aggregation
- The "calnexin cycle"
- UGGT - the folding "sensor" of the calnexin cycle
- The observed functions of Cnx and Crt
- Polypeptide-based interactions of Cnx/Crt
- Polypeptide-based interactions in vitro
- Characterization of the polypeptide binding site
- Cnx and Crt possessing lectin & polypeptide sites
- Cnx/Crt dual-binding model of glycoprotein
- Two similar chaperones, differing substrates
- Role of ERp57 in Cnx/Crt glycoprotein folding
- ERp57 functions with calnexin and calreticulin
- Interaction with a folding glycoprotein
- Ternary complex of ERp57, calnexin and substrate
- ERp57 receives most substrates from Cnx/Crt
- ERp57 role in glycoprotein folding by Cnx/Crt
- Peptidyl prolyl isomerases in the ER
- Functions of peptidyl prolyl isomerases in the ER
- Cyclophilin B interacts with Cnx/Crt
- Model of glycoprotein folding
- ER-associated degradation (ERAD)
- Recognition of misfolded glycoproteins
- The glyco code of the ER
- Recruitment to the retrotranslocon
- 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
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.Export Citation (RIS)
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.
Role of calnexin and calreticulin in protein homeostasis within the endoplasmic reticulum
Published on February 2, 2012
56 min
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