Related Experiment Video
Updated: Feb 24, 2026

08:12
High-throughput Screening for Protein-based Inheritance in S. cerevisiae
Published on: August 8, 2017
6.8K
Functions of the Prion Protein
Théo Z Hirsch1, Séverine Martin-Lannerée1, Sophie Mouillet-Richard1
1INSERM UMR 1124, Paris, France; Université Paris Descartes, Sorbonne Paris Cité, UMR 1124, Paris, France.
Progress in Molecular Biology and Translational Science
|August 26, 2017
Summary
The cellular prion protein (PrPC) is vital for numerous biological processes, including neuronal homeostasis and cell signaling. Understanding its diverse functions is key to addressing prion and Alzheimer's diseases.
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- The cellular prion protein (PrPC) was initially overlooked in favor of prion pathogenesis.
- Interest in PrPC functions surged due to its relevance in prion and Alzheimer's diseases.
- PrPC is now recognized for its involvement in diverse biological processes.
Purpose of the Study:
- To provide an overview of current knowledge on PrPC functions.
- To explore PrPC roles from the animal to the molecular scale.
- To identify knowledge gaps for future research.
Main Methods:
- Literature review and synthesis of existing research on PrPC functions.
- Analysis of PrPC involvement in various biological processes.
- Investigation of PrPC's role in cell signaling pathways.
Main Results:
- PrPC is implicated in neuronal homeostasis, stem cell fate, stress protection, and cell adhesion.
- These diverse functions are mediated through PrPC's involvement in cell signaling.
- PrPC's roles span multiple biological scales, from organismal to molecular.
Conclusions:
- The cellular prion protein (PrPC) plays a critical and multifaceted role in cellular biology.
- Understanding PrPC's signaling functions is crucial for comprehending its involvement in diseases.
- Further research is needed to fully elucidate the scope and mechanisms of PrPC functions.
Related Concept Videos
Amyloid Fibrils
12.1K
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.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
12.1K
Amyloid Fibrils
6.8K
6.8K
The Unfolded Protein Response
6.6K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
6.6K
Regulation of the Unfolded Protein Response
3.1K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
3.1K
Bacterial Protein Maturation
614
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...
614
Subviral Agents
642
Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
642

