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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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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

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Post-translational modifications in prion diseases.

Chloé Bizingre1,2, Clara Bianchi1,2, Anne Baudry1,2

  • 1INSERM UMR-S 1124, Paris, France.

Frontiers in Molecular Neuroscience
|July 16, 2024
PubMed
Summary
This summary is machine-generated.

Post-translational modifications (PTMs) are crucial for protein function but abnormal PTMs can cause diseases. This review explores how PTMs influence prion protein conversion and neurodegeneration, identifying potential drug targets.

Keywords:
PDK1 (PDPK1)PDK4ROCKneurodegenerative diseasesphosphorylationsialylationsignalingα-Secretases

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Protein Misfolding Cyclic Amplification of Prions
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Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • Post-translational modifications (PTMs) are vital for protein function and cellular homeostasis.
  • Aberrant PTMs are linked to various diseases, including neurodegenerative disorders.
  • The cellular prion protein (PrP C) undergoes a pathogenic conformational conversion (PTCC) into prions (PrP Sc), leading to neurodegeneration.

Purpose of the Study:

  • To review known PrP C PTMs that influence its conversion into pathogenic PrP Sc.
  • To summarize the impact of PrP C PTCC on the plasma membrane interactome and downstream effectors.
  • To discuss potential therapeutic strategies targeting these effectors for prion diseases.

Main Methods:

  • Literature review of PTMs affecting PrP C conversion.
  • Analysis of PrP C interactome alterations during PTCC.
  • Identification of intracellular protein effectors involved in neurodegeneration.

Main Results:

  • Specific PrP C PTMs modulate the conversion to PrP Sc.
  • PrP C PTCC disrupts the plasma membrane interactome and affects intracellular signaling pathways.
  • Altered PTMs contribute to the abnormal activation or trafficking of downstream protein effectors, promoting neurodegeneration.

Conclusions:

  • Understanding PrP C PTMs is crucial for deciphering prion disease pathogenesis.
  • Targeting downstream protein effectors affected by altered PTMs offers a promising therapeutic avenue for prion diseases.
  • These findings may extend to other neurodegenerative conditions.