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- Title
Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells
- Authors
Monnet, Céline; Gavard, Julie; Mège, René-Marc; Sobel, André
- Abstract
The physiological role of the prion protein is largely unknown. Here, clustering of prion at the surface of GT1-7 cells was observed upon anti-prion antibody treatments. This clustering was associated with a rapid and transient phosphorylation of the mitogen activated protein kinases (MAPKs) extracellular receptor kinases 1 and 2 (ERK1/2), and also of the microtubule-destabilizing protein stathmin at serine 16. The specificity of this antibody-mediated activation was ascertained by its inhibition by prion small interfering RNA. The phosphorylation of ERK1/2 but not that of stathmin was abolished by the MAPK/ERK kinase 1 inhibitor U0126, whereas both signaling pathways were blocked by the specific inhibitor of the epidermal growth factor receptor AG1478, suggesting the likely recruitment of this receptor upon prion clustering.
- Subjects
AMINO acids; PEPTIDES; NEUROPLASTICITY; PHYSIOLOGICAL adaptation
- Publication
FEBS Letters, 2004, Vol 576, Issue 1/2, p114
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2004.08.076