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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
- Concept of a molecular chaperone
- Saccharomyces cerevisiae
- TAP tag pull-downs (C-TAP)
- Mapping chaperon interaction network in yeast
- General principles: protein chaperon interaction
- Top MIPS complexes interacting with chaperons
- Top Pfam domains interacting with chaperons
- Chaperon-chaperon interactions
- Interactor overlap between two chaperones
- Single vs. multiple pathways model (1)
- Single vs. multiple pathways model (2)
- New cellular pathways modulated by chaperones
- Hsp90 and the conserved R2TP complex
- Hsp90: overview
- Integrated proteomics approaches
- 2H Two-hybrid screen using an ordered array
- TA tag pull-downs (forward and reverse)
- SGA Synthetic lethal screen
- GS Geldanamycin screen
- Hsp90 putatively interacts with 627 proteins
- Venn diagram
- Hsp90 putatively interaction (1)
- Hsp90 putatively interaction (2)
- Origin of synthetically lethal proteins with HSP90
- Proteomic data verification
- Biochemistry of individual proteins/systems
- Interesting ORF characteristics
- Tah1 and Pih1
- NMR structure of Tah1-MEEVD
- Hsp90-Tah1-Pih1 form a ternary complex
- Hsp90-Tah1-Pih1 complex function
- Hsp90 maintains the stability of Pih1
- Hsp90-Tah1 stabilize Pih1 in vivo (1)
- Hsp90-Tah1 stabilize Pih1 in vivo (2)
- Tah1 acts as a cofactor for HSP90
- Tah1 & Pih1 target HSP90 to specific proteins
- What is the function of the R2TP complex?
- R2P role in the cell
- Nop58 genetically interacts with R2TP
- The simplified view
- Box C/D snoRNP assembly
- rRNA and snoRNA accumulation (1)
- rRNA and snoRNA accumulation (2)
- Proposed model
- Summary
- Funding
- Thank you
Topics Covered
- Large scale proteomic screening in yeast
- The TAP-tag pulldown approach
- Understanding the principles governing protein homeostasis
- Mapping the network of the Hsp90 chaperone using physical and genetic interaction screens
- Unraveling the role of Hsp90 in pre-rRNA processing
Talk Citation
Houry, W.A. (2012, February 2). Mapping the molecular chaperone interaction network in yeast [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved April 19, 2025, from https://doi.org/10.69645/NNSB2557.Export Citation (RIS)
Publication History
- Published on February 2, 2012
Financial Disclosures
- Prof. Walid A. Houry has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.