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Background  The cellular prion protein, PrP C , is GPI anchored and abundant in lipid rafts. The absolute requirement of PrP C  in neurodegeneration associated to prion diseases is well established. However, the function of this ubiquitous protein is still puzzling. Our previous work using the 1C11 neuronal model, provided evidence that PrP C  acts as a cell surface receptor. Besides a ubiquitous signaling function of PrP C , we have described a neuronal specificity pointing to a role of PrP C  in neuronal homeostasis. 1C11 cells, upon appropriate induction, engage into neuronal differentiation programs, giving rise either to serotonergic (1C11 5-HT ) or noradrenergic (1C11 NE ) derivatives.    Methodology/Principal Findings  The neuronal specificity of PrP C  signaling prompted us to search for PrP C  partners in 1C11-derived bioaminergic neuronal cells. We show here by immunoprecipitation an association of PrP C  with an 80 kDa protein identified by mass spectrometry as the tissue non-specific alkaline phosphatase (TNAP). This interaction occurs in lipid rafts and is restricted to 1C11-derived neuronal progenies. Our data indicate that TNAP is implemented during the differentiation programs of 1C11 5-HT  and 1C11 NE  cells and is active at their cell surface. Noteworthy, TNAP may contribute to the regulation of serotonin or catecholamine synthesis in 1C11 5-HT  and 1C11 NE  bioaminergic cells by controlling pyridoxal phosphate levels. Finally, TNAP activity is shown to modulate the phosphorylation status of laminin and thereby its interaction with PrP.    Conclusion/Significance  The identification of a novel PrP C  partner in lipid rafts of neuronal cells favors the idea of a role of PrP in multiple functions. Because PrP C  and laminin functionally interact to support neuronal differentiation and memory consolidation, our findings introduce TNAP as a functional protagonist in the PrP C -laminin interplay. The partnership between TNAP and PrP C  in neuronal cells may provide new clues as to the neurospecificity of PrP C  function.

The Cellular Prion Protein Interacts with the Tissue Non-Specific Alkaline Phosphatase in Membrane Microdomains of Bioaminergic Neuronal Cells