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Related Concept Videos

Huntington Disease l: Introduction01:21

Huntington Disease l: Introduction

Huntington disease or HD is a progressive, fatal neurodegenerative disorder inherited in an autosomal dominant pattern.PathophysiologyIt is caused by expansion of the CAG trinucleotide repeat in the HTT gene on chromosome 4 (4p16.3), producing an abnormal huntingtin protein with an expanded polyglutamine tract. This misfolded protein disrupts cellular function, leading to neuronal death. Normal alleles have ≤26 repeats, 27–35 are intermediate (risk of expansion), 36–39 show reduced penetrance,...

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Related Experiment Video

Updated: May 9, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
07:08

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species

Published on: February 27, 2018

TRiC's tricks inhibit huntingtin aggregation.

Sarah H Shahmoradian1, Jesus G Galaz-Montoya, Michael F Schmid

  • 1Department of Molecular Physiology and Biophysics , Baylor College of Medicine , Houston , United States ; National Center for Macromolecular Imaging, and the Verna and Marrs McLean Department of Biochemistry and Molecular Biology , Baylor College of Medicine , Houston , United States.

Elife
|July 16, 2013
PubMed
Summary
This summary is machine-generated.

The eukaryotic chaperonin TRiC (TCP1-ring complex) inhibits Huntington's disease protein aggregation by capping fibril tips and encapsulating oligomers, offering new therapeutic insights.

Keywords:
AmyloidCryo electron microscopy (cryoEM)Cryo electron tomography (cryoET)HuntingtinNoneSingle particle tomography (SPT)TRiC chaperonin

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Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
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Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

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Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System
10:52

Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System

Published on: December 10, 2021

Related Experiment Videos

Last Updated: May 9, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
07:08

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species

Published on: February 27, 2018

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
11:22

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

Published on: June 27, 2018

Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System
10:52

Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System

Published on: December 10, 2021

Area of Science:

  • Biochemistry
  • Neuroscience
  • Structural Biology

Background:

  • Huntington's disease involves cell death caused by mutated huntingtin protein aggregation.
  • The eukaryotic chaperonin TRiC (TCP1-ring complex) shows potential in inhibiting this aggregation.
  • Understanding chaperone interactions with mutant huntingtin is crucial for therapeutic development.

Purpose of the Study:

  • To structurally characterize the aggregation of mutant huntingtin exon 1 (mhttQ51).
  • To resolve the 3-D structures of TRiC interacting with mhttQ51 aggregates.
  • To elucidate the mechanisms by which TRiC modulates mhttQ51 aggregation.

Main Methods:

  • Cryo-electron microscopy (cryoEM) and single particle cryo-electron tomography (SPT) were employed.
  • Characterization of fibrillar aggregate growth of mhttQ51.
  • 3-D structural analysis of TRiC-mhttQ51 interactions.

Main Results:

  • TRiC was observed to cap the tips of mhttQ51 fibrils through its apical domains.
  • TRiC was also found to encapsulate smaller mhtt oligomers within its central chamber.
  • These findings provide structural evidence for TRiC's inhibitory role in mhttQ51 aggregation.

Conclusions:

  • TRiC employs dual mechanisms to inhibit mutant huntingtin aggregation.
  • Structural insights into TRiC-mhttQ51 interactions pave the way for targeted Huntington's disease therapies.