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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

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Updated: Jul 20, 2026

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
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Published on: December 17, 2021

The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions.

Stephen Tam1, Ron Geller, Christoph Spiess

  • 1Biophysics Graduate Program, Stanford University, Stanford, California 94305, USA.

Nature Cell Biology
|September 19, 2006
PubMed
Summary

The chaperonin TRiC (also known as CCT) prevents toxic protein aggregation in neurodegenerative diseases like Huntington's. Enhancing TRiC or its subunit CCT1 reduces harmful protein clumps and neuronal cell death.

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Last Updated: Jul 20, 2026

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06:49

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Growth Assays to Assess Polyglutamine Toxicity in Yeast
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Caenorhabditis elegans as a Model System for Discovering Bioactive Compounds Against Polyglutamine-Mediated Neurotoxicity
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Caenorhabditis elegans as a Model System for Discovering Bioactive Compounds Against Polyglutamine-Mediated Neurotoxicity

Published on: September 21, 2021

Area of Science:

  • Molecular biology
  • Neuroscience
  • Protein biochemistry

Background:

  • Protein misfolding and aggregation, particularly of polyglutamine-expanded huntingtin (Htt), are hallmarks of neurodegenerative diseases.
  • The cellular mechanisms preventing such aggregation are not fully understood.

Purpose of the Study:

  • To investigate the role of the chaperonin TRiC/CCT in the aggregation of polyglutamine-expanded huntingtin.
  • To explore the therapeutic potential of TRiC/CCT in neurodegenerative disorders.

Main Methods:

  • Yeast and mammalian cell culture models.
  • Protein interaction studies.
  • In vivo and in vitro aggregation assays.
  • Neuronal cell toxicity assessments.

Main Results:

  • TRiC/CCT directly interacts with and inhibits the aggregation of polyglutamine-expanded Htt.
  • TRiC/CCT depletion exacerbates Htt aggregation.
  • Overexpression of CCT1 remodels Htt aggregates and reduces Htt-induced toxicity in neuronal cells.

Conclusions:

  • TRiC/CCT plays a crucial role in preventing the aggregation of pathogenic proteins like Htt.
  • TRiC/CCT may act early in protein biogenesis to avert toxic conformations.
  • Targeting the TRiC/CCT-Htt interaction, specifically the CCT1 substrate-binding domain, offers a potential therapeutic strategy for neurodegenerative diseases.