Journal
FEBS LETTERS
Volume 576, Issue 1-2, Pages 114-118Publisher
WILEY
DOI: 10.1016/j.febslet.2004.08.076
Keywords
EGF receptor; MAP kinase; clustering; prion signaling; stathmin; siRNA
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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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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