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J. Biol. Chem., Vol. 276, Issue 48, 44604-44612, November 30, 2001
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From the Max von Pettenkofer Institute, Department of Virology,
Gene Center Munich, Ludwig Maximilians University of Munich,
Feodor-Lynen-Strasse 25, D-81377 Munich, Germany
The cellular prion protein
(PrPC) is a conserved glycoprotein predominantly
expressed in neuronal cells. Its purpose in living cells is still
enigmatic. To elucidate on its cellular function, we performed a yeast
two-hybrid screen for interactors. We used murine PrPC
(amino acids 23-231) as bait to search a mouse brain cDNA
expression library. Several interaction partners were identified. Three
of them with a high homology to known sequences were further
characterized. These candidates were the neuronal phosphoprotein
synapsin Ib, the adaptor protein Grb2, and the still uncharacterized
prion interactor Pint1. The in vivo interaction of the
three proteins with PrPC was confirmed by
co-immunoprecipitation assays with recombinant and authentic proteins
in mammalian cells. The binding regions were mapped using truncated PrP
constructs. As both synapsin Ib and Grb2 are implicated in neuronal
signaling processes, our findings further strengthen the
putative role of the prion protein in signal transduction.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AY029599.
PrPC Directly Interacts with Proteins Involved in
Signaling Pathways*
*
This work was supported by Deutsche Forschungsgemeinschaft
Grant Scha 594-3/3.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
49-89-21806855; Fax: 49-89-21806898; E-mail:
schaetzl@lmb.uni-muenchen.de.
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