Publication Date:
2000-09-16
Description:
The cellular prion protein PrPc is a glycosylphosphatidylinositol-anchored cell-surface protein whose biological function is unclear. We used the murine 1C11 neuronal differentiation model to search for PrPc-dependent signal transduction through antibody-mediated cross-linking. A caveolin-1-dependent coupling of PrPc to the tyrosine kinase Fyn was observed. Clathrin might also contribute to this coupling. The ability of the 1C11 cell line to trigger PrPc-dependent Fyn activation was restricted to its fully differentiated serotonergic or noradrenergic progenies. Moreover, the signaling activity of PrPc occurred mainly at neurites. Thus, PrPc may be a signal transduction protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mouillet-Richard, S -- Ermonval, M -- Chebassier, C -- Laplanche, J L -- Lehmann, S -- Launay, J M -- Kellermann, O -- New York, N.Y. -- Science. 2000 Sep 15;289(5486):1925-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Differenciation Cellulaire, CNRS-Institut Pasteur, 75724 Paris Cedex 15, France. srichard@pasteur.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10988071" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Caveolin 1
;
*Caveolins
;
Cell Compartmentation
;
Cell Differentiation
;
Enzyme Activation
;
Membrane Proteins/metabolism
;
Mice
;
Neurons/cytology/metabolism
;
PrPC Proteins/*metabolism
;
Proto-Oncogene Proteins/metabolism
;
Proto-Oncogene Proteins c-fyn
;
*Signal Transduction
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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