p(HBP:"Tau aggregates") positiveCorrelation p(HGNC:MAPT, pmod(Ph, Ser, 324))

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PubMed:28760828

Our findings indicate that several acetylation sites in tau are responsive to HDAC6 and that acetylation on Lys-321 (within a KCGS motif) is both essential for acetylation-mediated inhibition of tau aggregation in vitro and a molecular tactic for preventing phosphorylation on the downstream Ser-324 residue. Tau phosphorylation of Ser-324 (pSer-324) has not previously been evaluated in the context of tauopathy, and here we observed increased deposition of pSer-324-positive tau both in mouse models of tauopathy and in patients with Alzheimer's disease. These findings uncover a novel acetylation-phosphorylation switch at Lys-321/Ser-324 that coordinately regulates tau polymerization and function.

Related Edges 3

• p(HGNC:MAPT, pmod(Ac, Lys, 321)) decreases p(HBP:"Tau aggregates")
• p(HGNC:MAPT, pmod(Ac, Lys, 321)) decreases p(HGNC:MAPT, pmod(Ph, Ser, 324))
• p(HGNC:MAPT, pmod(Ph, Ser, 324)) positiveCorrelation p(HBP:"Tau aggregates")

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