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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
- Heat shock genes and proteins discovery
- Heat shock elements and transcription factor 1
- Conditions for activation of HSF-1
- 5 different heat shock protein families
- Some families are nor HSF-1 regulated
- HSPs are molecular chaperones
- HSPs and folding of nascent proteins
- Heat-induced HSP up-regulation
- HSP70 and toxicity protection
- HSPs and mutant proteins
- HSPs: expansion and functional diversification
- Interaction between different HSP families
- HSP70 machines
- Functional specificity via different HSP70s
- Functional specificity via different NEFs
- Functional specificity via different DNAJs
- Functional classification of DNAJ proteins
- Promiscuous client binding in DNAJ proteins
- Ydj1 and Sis1/DNAJB1 generally promote refolding
- DNAJB2 directs clients to degradation
- Selective client binding
- DNAJs without client binding for tethering HSP70
- DNAJC2
- Functional specificity beyond DNAJs
- The HSP70 machine and folding diseases
- PolyQ diseases
- Recognizing HSPs in polyQ disease
- DNAJB6/8 suppressors of poly-Q aggregation
- DNAJB6/8 protect against poly-Q toxicity
- Deletion of SSF-SST region of DNAJB8
- DNAJB6 / DNAJB8 interact with HDACs
- HDAC4 is required for DNAJB6/8 function
- DNAJB8 acetylation
- C-terminal lysines involved in activity of DNAJB8
- DNAJB6 prevents polyQ aggregation in vitro
- DNAJB6/8 prevent polyQ aggregation in cells
- A model of prevention of polyQ aggregation
- HSPB expansion and functional diversification
- HSPB alpha-crystalline domain
- Human HSPB family
- Refolding vs. polyQ aggregation
- Canonical mechanism of refolding
- Non-canonical mechanism of refolding
- Summary
- Acknowledgements
- References
Topics Covered
- Heat shock proteins
- Regulation and chaperone activity
- Several protein families with many different members
- DNAJ family
- Regulation of differentiation of HSP machines to drive client specificity and differential client processing
- Involvement in folding, proteasomal degradation, autophagy
- Potent suppressors of protein deposit diseases, e.g. CAG repeat diseases
Talk Citation
Kampinga, H. (2012, February 2). Human heat shock protein families [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved March 29, 2024, from https://hstalks.com/bs/2212/.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Herman Kampinga has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.