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Amyloid Fibrils03:03

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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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...
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Related Experiment Video

Updated: May 5, 2026

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model
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α-Synuclein as a ferrireductase.

David R Brown1

  • 1*Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, U.K.

Biochemical Society Transactions
|November 22, 2013
PubMed
Summary

Alpha-synuclein, a protein linked to Parkinson's disease, may have its function defined by its newly discovered ability to reduce iron using copper. This finding offers new insights into neurodegenerative disease mechanisms.

Area of Science:

  • Neurobiology
  • Protein Biochemistry
  • Neurodegenerative Diseases

Background:

  • Many proteins implicated in neurodegenerative diseases, such as alpha-synuclein (α-synuclein), have poorly understood functions.
  • Alpha-synuclein is notably associated with Parkinson's disease and is now recognized as a metal-binding protein.
  • Its function may be linked to cofactor binding, with recent suggestions pointing to a specific catalytic activity.

Purpose of the Study:

  • To review the evidence for alpha-synuclein's proposed function in iron reduction.
  • To explore the implications of this function for understanding Parkinson's disease.

Main Methods:

  • This review synthesizes existing research and recent findings.
  • It discusses the catalytic activity of alpha-synuclein involving copper and iron reduction.

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  • Evidence supporting this proposed function is critically examined.

    • Main Results:

    • Recent studies suggest alpha-synuclein can reduce iron, utilizing copper as a catalytic center.
    • This catalytic activity provides a potential explanation for the protein's function.
    • The interaction of alpha-synuclein with metals like iron and copper is a key focus.

    Conclusions:

    • The proposed function of alpha-synuclein in iron reduction offers a new perspective on its biological role.
    • Understanding this function may be crucial for unraveling the pathogenesis of Parkinson's disease.
    • Further research into alpha-synuclein's metal-binding properties and catalytic activities is warranted.