act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(MGI:Mapt, pmod(Ph, Thr, 205))

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PubMed:24113872

Using mass spectrometry, we identified multiple sites on recombinant tau that are phosphorylated by LRRK2 in vitro, including pT149 and pT153, which are phospho-epitopes that to date have been largely unexplored. Importantly, we demonstrate that expression of transgenic LRRK2 in a mouse model of tauopathy increased the aggregation of insoluble tau and its phosphorylation at T149, T153, T205, and S199/S202/T205 epitopes.

Related Edges 6

• p(HGNC:LRRK2) positiveCorrelation path(MESH:"Parkinson Disease")
• act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(MGI:Mapt, pmod(Ph, Thr, 149))
• act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(MGI:Mapt, pmod(Ph, Thr, 153))
• act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(HBP:"Tau epitope, AT8")
• act(p(HGNC:LRRK2), ma(kin)) directlyIncreases p(HBP:"Tau aggregates")
• path(MESH:"Parkinson Disease") positiveCorrelation p(HGNC:LRRK2)

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