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Science 289 (5486): 1925-1928

Copyright © 2000 by the American Association for the Advancement of Science

Signal Transduction Through Prion Protein

S. Mouillet-Richard,1* M. Ermonval,1 C. Chebassier,12 J. L. Laplanche,2 S. Lehmann,3 J. M. Launay,2 O. Kellermann1

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.

1 Différenciation Cellulaire, CNRS-Institut Pasteur, 75724 Paris Cedex 15, France.
2 CR Claude Bernard, Service de Biochimie, Hôpital Lariboisière, 75009 Paris, and Faculté de Pharmacie, 75005 Paris, France.
3 IGH du CNRS, UPR 1142, 34396 Montpellier Cedex 5, France.
*   To whom correspondence should be addressed. E-mail: srichard{at}pasteur.fr


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Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection.
S. M. Zanata, M. H. Lopes, A. F. Mercadante, G. N. M. Hajj, L. B. Chiarini, R. Nomizo, A. R. O. Freitas, A. L. B. Cabral, K. S. Lee, M. A. Juliano, et al. (2002)
EMBO J. 21, 3307-3316
   Abstract »    Full Text »    PDF »
Cellular prion protein transduces neuroprotective signals.
L. B. Chiarini, A. R. O. Freitas, S. M. Zanata, R. R. Brentani, V. R. Martins, and R. Linden (2002)
EMBO J. 21, 3317-3326
   Abstract »    Full Text »    PDF »
Mutant prion protein acquires resistance to protease in mouse neuroblastoma cells.
C. Wegner, A. Romer, R. Schmalzbauer, H. Lorenz, O. Windl, and H. A. Kretzschmar (2002)
J. Gen. Virol. 83, 1237-1245
   Abstract »    Full Text »    PDF »
Cutting Edge: Recruitment of the Ancestral fyn Gene During Emergence of the Adaptive Immune System.
C. Picard, A. Gilles, P. Pontarotti, D. Olive, and Y. Collette (2002)
J. Immunol. 168, 2595-2598
   Abstract »    Full Text »    PDF »
PrPc Expression Influences the Establishment of Herpes Simplex Virus Type 1 Latency.
A. M. Thackray and R. Bujdoso (2002)
J. Virol. 76, 2498-2509
   Abstract »    Full Text »    PDF »
Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration.
G. R. Mallucci, S. Ratte, E. A. Asante, J. Linehan, I. Gowland, J. G. R. Jefferys, and J. Collinge (2002)
EMBO J. 21, 202-210
   Abstract »    Full Text »    PDF »
The normal cellular prion protein is strongly expressed by myeloid dendritic cells.
J. Burthem, B. Urban, A. Pain, and D. J. Roberts (2001)
Blood 98, 3733-3738
   Abstract »    Full Text »    PDF »
Prion Protein Fragment PrP-(106-126) Induces Apoptosis via Mitochondrial Disruption in Human Neuronal SH-SY5Y Cells.
C. N. O'Donovan, D. Tobin, and T. G. Cotter (2001)
J. Biol. Chem. 276, 43516-43523
   Abstract »    Full Text »    PDF »
Deletion of {beta}-Strand and {alpha}-Helix Secondary Structure in Normal Prion Protein Inhibits Formation of Its Protease-Resistant Isoform.
I. Vorberg, K. Chan, and S. A. Priola (2001)
J. Virol. 75, 10024-10032
   Abstract »    Full Text »    PDF »
The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein.
S. Gauczynski, J.-M. Peyrin, S. Haik, C. Leucht, C. Hundt, R. Rieger, S. Krasemann, J.-P. Deslys, D. Dormont, C. I. Lasmezas, et al. (2001)
EMBO J. 20, 5863-5875
   Abstract »    Full Text »    PDF »
Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor.
C. Hundt, J.-M. Peyrin, S. Haik, S. Gauczynski, C. Leucht, R. Rieger, M. L. Riley, J.-P. Deslys, D. Dormont, C. I. Lasmezas, et al. (2001)
EMBO J. 20, 5876-5886
   Abstract »    Full Text »    PDF »
Prion Protein Protects Human Neurons against Bax-mediated Apoptosis.
Y. Bounhar, Y. Zhang, C. G. Goodyer, and A. LeBlanc (2001)
J. Biol. Chem. 276, 39145-39149
   Abstract »    Full Text »    PDF »
Prion protein: Evolution caught en route.
P. Tompa, G. E. Tusnady, M. Cserzo, and I. Simon (2001)
PNAS 98, 4431-4436
   Abstract »    Full Text »    PDF »
Prion proteins and the gut: une liaison dangereuse?.
A N SHMAKOV and S GHOSH (2001)
Gut 48, 443-447
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Mapping the early steps in the pH-induced conformational conversion of the prion protein.
D. O. V. Alonso, S. J. DeArmond, F. E. Cohen, and V. Daggett (2001)
PNAS 98, 2985-2989
   Abstract »    Full Text »    PDF »
Two different neurodegenerative diseases caused by proteins with similar structures.
H. Mo, R. C. Moore, F. E. Cohen, D. Westaway, S. B. Prusiner, P. E. Wright, and H. J. Dyson (2001)
PNAS 98, 2352-2357
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Cleavage of the Amino Terminus of the Prion Protein by Reactive Oxygen Species.
H. E. M. McMahon, A. Mange, N. Nishida, C. Creminon, D. Casanova, and S. Lehmann (2001)
J. Biol. Chem. 276, 2286-2291
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The Prion Protein Has RNA Binding and Chaperoning Properties Characteristic of Nucleocapsid Protein NCp7 of HIV-1.
C. Gabus, E. Derrington, P. Leblanc, J. Chnaiderman, D. Dormont, W. Swietnicki, M. Morillas, W. K. Surewicz, D. Marc, P. Nandi, et al. (2001)
J. Biol. Chem. 276, 19301-19309
   Abstract »    Full Text »    PDF »
Addition of a Glycophosphatidylinositol to Acetylcholinesterase. PROCESSING, DEGRADATION, AND SECRETION.
F. Coussen, A. Ayon, A. Le Goff, J. Leroy, J. Massoulie, and S. Bon (2001)
J. Biol. Chem. 276, 27881-27892
   Abstract »    Full Text »    PDF »

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