Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 38, Pages 32040-32053Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.401240
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Funding
- Canadian Institutes of Health Research
- Alzheimer Society of Canada
- Groupe de Recherche sur le Systeme Nerveux Central
- Department of Physiology, Universite de Montreal
- Fonds de la Recherche en Sante du Quebec
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Amyloid-beta 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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