Related Experiment Video

Updated: Jul 2, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

CREB-dependent gene regulation by prion protein: impact on MMP-9 and beta-dystroglycan

Elodie Pradines1, Damien Loubet, Benoît Schneider

  • 1Différenciation, Cellules souches et Prions, CNRS FRE2937 - INSERM U747, Institut André Lwoff, 7 rue Guy Moquet, BP8, 94801 Villejuif Cedex, France.

Cellular Signalling
|August 23, 2008
PubMed

Insights

The cellular prion protein (PrP(C)) plays a signaling role in neuronal cells, influencing transcription factors like CREB and immediate early genes, impacting cell survival and plasticity.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • The physiological role of the cellular prion protein (PrP(C)) is not fully understood.
  • PrP(C) dysfunction is implicated in Transmissible Spongiform Encephalopathies (TSEs).

Purpose of the Study:

  • To elucidate the signaling function of PrP(C) in neuronal cells.
  • To investigate the molecular mechanisms downstream of PrP(C) activation.

Main Methods:

  • Utilized the 1C11 neuroectodermal cell line and its neuronal progenies (1C11(5-HT) and 1C11(NE)).
  • Employed antibody-mediated PrP(C) ligation to study downstream signaling pathways.
  • Analyzed the activation of transcription factors (CREB) and gene expression (Egr-1, c-fos, MMP-9, TIMP-1).

Main Results:

  • PrP(C) ligation activates the CREB transcription factor via MAPK ERK1/2 signaling in precursor and neuronal cells.
  • PrP(C)-dependent CREB activation induces Egr-1 and c-fos transcription, crucial for cell survival and plasticity.
  • PrP(C) signaling regulates the expression of MMP-9 and TIMP-1 in neuronal cells.
  • PrP(C) control over MMP-9 affects beta-dystroglycan processing.

Conclusions:

  • PrP(C) functions as a signaling molecule, mediating cytoprotection and neuronal plasticity.
  • Identified molecular pathways linking PrP(C) to gene transcription and protein processing.
  • Provides insights into the normal function of PrP(C) and its potential role in neurological conditions.

More Related Videos

CRISPR/Cas9 Technology in Restoring Dystrophin Expression in iPSC-Derived Muscle Progenitors07:44

CRISPR/Cas9 Technology in Restoring Dystrophin Expression in iPSC-Derived Muscle Progenitors

Published on: September 14, 2019

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...