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

被引：196

作者：

Mondragon-Rodriguez, Siddhartha ^{[1
]}

Trillaud-Doppia, Emilie ^{[1
]}

Dudilot, Anthony ^{[1
]}

Bourgeois, Catherine ^{[1
]}

Lauzon, Michel ^{[2
]}

Leclerc, Nicole ^{[2
]}

Boehm, Jannic ^{[1
]}

机构：

[1] Univ Montreal, Dept Physiol, Montreal, PQ H3T 1J4, Canada

[2] Univ Montreal, Dept Pathol & Biol Cellulaire, Grp Rech Syst Nerveux Cent, Montreal, PQ H3T 1J4, Canada

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2012年 / 287卷 / 38期

基金：

加拿大健康研究院;

关键词：

AMYLOID PRECURSOR PROTEIN; LONG-TERM POTENTIATION; ALZHEIMERS-DISEASE; TRANSGENIC MICE; A-BETA; TRAFFICKING; TRANSMISSION; DEPRESSION; EXPRESSION; PLASTICITY;

D O I：

10.1074/jbc.M112.401240

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：32040 / 32053

页数：14

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