bp(MESH:"Long-Term Potentiation") negativeCorrelation p(HGNC:WWC1)

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PubMed:27041503

Here we report abnormal acetylation of K274 and K281 on tau, identified in AD brains, promotes memory loss and disrupts synaptic plasticity by reducing postsynaptic KIdney/BRAin (KIBRA) protein, a memory-associated protein.Transgenic mice expressing human tau with lysine-to-glutamine mutations to mimic K274 and K281 acetylation (tauKQ) exhibit AD-related memory deficits and impaired hippocampal long-term potentiation (LTP). TauKQ reduces synaptic KIBRA levels and disrupts activity-induced postsynaptic actin remodeling and AMPA receptor insertion. The LTP deficit was rescued by promoting actin polymerization or by KIBRA expression. In AD patients with dementia, we found enhanced tau acetylation is linked to loss of KIBRA.

Related Edges 10

• bp(GO:"actin filament polymerization") negativeCorrelation bp(MESH:"Long-Term Potentiation")
• bp(GO:memory) positiveCorrelation bp(MESH:"Long-Term Potentiation")
• bp(MESH:"Long-Term Potentiation") negativeCorrelation bp(GO:"actin filament polymerization")
• bp(MESH:"Long-Term Potentiation") positiveCorrelation bp(GO:memory)
• p(HGNC:MAPT, pmod(Ac, Lys, 281)) decreases p(HGNC:WWC1)
• p(HGNC:MAPT, pmod(Ac, Lys, 281)) decreases bp(GO:"actin filament polymerization")
• p(HGNC:MAPT, pmod(Ac)) decreases p(HGNC:WWC1)
• p(HGNC:MAPT, pmod(Ac, Lys, 274)) decreases p(HGNC:WWC1)
• p(HGNC:MAPT, pmod(Ac, Lys, 274)) decreases bp(GO:"actin filament polymerization")
• p(HGNC:WWC1) negativeCorrelation bp(MESH:"Long-Term Potentiation")

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