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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
- Importance of molecular chaperones
- Protein folding process
- Transitions during protein folding
- Protein folding in the cytosol
- Chaperone assisted protein folding: history
- Protein folding in vitro and in mitochondria
- Protein folding is often competed by aggregation
- The cellular environment is highly crowded
- Chaperone-assisted protein folding in E. coli
- Reconstitution of GroEL-assisted folding
- Early electron micrographs of GroEL
- GroES binds to the ends of the GroEL cylinder
- GroEL and GroES function as a folding cage
- GroEL structure
- Which proteins need GroEL/GroES for folding?
- Identification of the GroEL interaction proteome
- Class III substrates are of low cellular abundance
- Cellular depletion of GroEL/ES
- Size distribution of class III proteins
- Enrichment of TIM beta/alpha-barrel fold
- GroEL substrates have complex structures
- Chaperonins provide a folding environment
- GroEL as part of cytosolic chaperone network
- Cooperation of GroEL with upstream chaperones
- A summarizing movie
- Acknowledgements
Topics Covered
- De novo protein folding and proteome maintenance critically depend on molecular chaperones
- Transitions during protein folding
- Chaperone assisted protein folding
- Productive protein folding is often competed by aggregation
- Reconstitution of GroEL-assisted folding
- GroEL and GroES function as a folding cage for proteins up to 60 kDa
- GroEL structure
- Which proteins need GroEL/GroES for folding?
- Identification of the GroEL interaction proteome
- Class III substrates are of relatively low cellular abundance but occupy most of the GroEL capacity
- Chaperonins provide a specialized folding environment with two functional elements: sequestration and steric confinement in a hydrophilic cage
- GroEL as part of the cytosolic chaperone network
Talk Citation
Hartl, F.U. (2021, September 15). The interaction network of the GroEL chaperonin [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved March 21, 2025, from https://doi.org/10.69645/DMXH8647.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Dr. F. Ulrich Hartl has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
The interaction network of the GroEL chaperonin
A selection of talks on Cell Biology
Transcript
Please wait while the transcript is being prepared...
0:00
How cells ensure the integrity of their proteome, and maintain protein homeostasis,
has emerged as one of the most fascinating and medically relevant areas of molecular cell biology.
This exciting development is the result of a paradigm shift in our understanding of how proteins fold in the cell,
which has occurred over the last two decades.
0:24
We no longer believe that newly-synthesized polypeptides fold in
a spontaneous process, solely dependent on
the steric information contained in the amino acid sequences.
Instead, it is clear that many proteins require assistance from molecular chaperones,
to realize their inbuilt potential to fold efficiently, and at a biologically relevant timescale.
This machinery is not only required for folding under normal conditions,
but also under various conditions of stress.
Moreover, chaperones are also linked with
important diseases in which proteins mis-fold and aggregate,
including some of the most debilitating neurodegenerative diseases.
The discovery of a particular class of molecular chaperones,
the so-called 'chaperonins', was critical in the development of these insights.
1:15
Protein folding is the final step in the information transfer from gene to functional protein,
and as such, it is arguably one of the most important processes in biology.
Folding is a complex search process, in which the linear information in
the amino acid sequence gives rise to
the defined and unique 3-dimensional conformation of a protein's native state.
1:40
In effect, folding is a polymer condensation process, in which
an astronomically large number of possible unfolded conformers
(shown here for the small protein Barnase) converge
rapidly through multiple pathways, to a set of so-called 'random globules'.
These are relatively compact conformations containing
secondary structure elements, but lacking defined tertiary interactions.
Further restriction in configurational entropy, through
the formation of native context, finally leads
this ensemble to the single defined structure of
the native state, in which hydrophobic amino acid residues are buried within a tightly-folded hydrophobic core.
There has been significant progress in recent years in
understanding the structural basis of protein folding,
but we're still unable to predict the three-dimensional structure of a protein just from its sequence.
How do cells solve the protein folding problem?