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Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells
- Source :
-
FEBS Letters . Oct2004, Vol. 576 Issue 1/2, p114-118. 5p. - Publication Year :
- 2004
-
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. [Copyright &y& Elsevier]
- Subjects :
- *AMINO acids
*PEPTIDES
*NEUROPLASTICITY
*PHYSIOLOGICAL adaptation
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 576
- Issue :
- 1/2
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 14649230
- Full Text :
- https://doi.org/10.1016/j.febslet.2004.08.076