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Interaction of Endogenous Tau Protein with Synaptic Proteins Is Regulated by N-Methyl-d-aspartate Receptor-dependent Tau Phosphorylation*

S. Mondragón-Rodríguez,Emilie Trillaud-Doppia,Anthony Dudilot,Catherine Bourgeois,M. Lauzon,N. Leclerc,Jannic Boehm

Published 2012 in Journal of Biological Chemistry

ABSTRACT

Background: Tau phosphorylation affects synaptic transmission, but the underlying mechanism remains elusive. Results: NMDA receptor activation leads to phosphorylation of endogenous tau, thereby regulating the interaction of tau with Fyn and postsynaptic scaffolding protein PSD95. Conclusion: Phosphorylation of tau controls the interaction of tau with the postsynaptic PSD95-Fyn-NMDA receptor complex leading to changes in synaptic activity. Significance: The here described physiological mechanism could go awry during the development of Alzheimer disease. Amyloid-β and tau protein are the two most prominent factors in the pathology of Alzheimer disease. Recent studies indicate that phosphorylated tau might affect synaptic function. We now show that endogenous tau is found at postsynaptic sites where it interacts with the PSD95-NMDA receptor complex. NMDA receptor activation leads to a selective phosphorylation of specific sites in tau, regulating the interaction of tau with Fyn and the PSD95-NMDA receptor complex. Based on our results, we propose that the physiologically occurring phosphorylation of tau could serve as a regulatory mechanism to prevent NMDA receptor overexcitation.

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