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J Biol Chem. 2012 Sep 14;287(38):32040-53. doi: 10.1074/jbc.M112.401240. Epub 2012 Jul 25.

Interaction of endogenous tau protein with synaptic proteins is regulated by N-methyl-D-aspartate receptor-dependent tau phosphorylation.

Author information

1
Département de Physiologie, Université de Montréal, Montréal, Québec H3T 1J4, Canada.

Abstract

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.

PMID:
22833681
PMCID:
PMC3442535
DOI:
10.1074/jbc.M112.401240
[Indexed for MEDLINE]
Free PMC Article

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