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Related Concept Videos

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Overview of Protein Sorting and Transport01:45

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Related Experiment Video

Updated: Oct 5, 2025

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
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Cysteine String Protein Controls Two Routes of Export for Misfolded Huntingtin.

Desmond Pink1, Julien Donnelier2, John D Lewis1,3

  • 1Nanostics Precision Health, Edmonton, AB, Canada.

Frontiers in Neuroscience
|January 24, 2022
PubMed
Summary
This summary is machine-generated.

Cysteine string protein alpha (CSPα) aids in exporting mutant huntingtin protein via extracellular vesicles (EVs). This finding is crucial for understanding Huntington's disease progression and EV involvement.

Keywords:
DnaJHuntington’s diseaseJDPexportmicroflow cytometrymolecular chaperone

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Last Updated: Oct 5, 2025

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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
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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Extracellular vesicles (EVs) mediate cell-to-cell transfer of disease-associated proteins in neurodegenerative diseases.
  • Mutant huntingtin protein with expanded polyglutamine tracts misfolds and forms toxic aggregates in Huntington's disease.
  • Cellular pathways for mutant huntingtin export via EVs are being identified.

Purpose of the Study:

  • To identify specific EV subpopulations involved in the cellular export of mutant huntingtin.
  • To investigate the role of molecular chaperones in the export of misfolded huntingtin cargo.
  • To understand the mechanisms of extracellular vesicle-mediated protein transmission in Huntington's disease.

Main Methods:

  • Expressed GFP-tagged 72Qhuntingtin exon 1 in cells to study EV-mediated export.
  • Analyzed extracellular vesicles (EVs) for the presence of mutant huntingtin cargo.
  • Assessed the role of cysteine string protein alpha (CSPα; DnaJC5) in facilitating cargo export.

Main Results:

  • Cysteine string protein alpha (CSPα) was found to facilitate the export of mutant huntingtin cargo.
  • Mutant huntingtin was exported in extracellular vesicles (EVs) of two size ranges: 180-240 nm and larger 10-30 μm vesicles.
  • CSPα plays a role in the trafficking of misfolded huntingtin via specific EV populations.

Conclusions:

  • Cysteine string protein alpha (CSPα) is a key facilitator of mutant huntingtin export via extracellular vesicles (EVs).
  • The study identifies specific EV sizes involved in the transport of toxic huntingtin protein.
  • Understanding this pathway is critical for developing therapeutic strategies for Huntington's disease.