a(CHEBI:staurosporine) decreases p(HGNC:MAPT, pmod(Ph, Ser, 262))

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PubMed:23001711

Several kinases such as microtubule-affinity regulating kinase (MARK), protein kinase A, calcium calmodulin kinase II, and checkpoint kinase 2 are known to phosphorylate tau on Ser(262) in vitro. In this study, we took advantage of the in situ proximity ligation assay to investigate the role of MARK2, one of the four MARK isoforms, in AD. We demonstrate that MARK2 interacts with tau and phosphorylates tau at Ser(262) in stably transfected NIH/3T3 cells expressing human recombinant tau. Staurosporine, a protein kinase inhibitor, significantly reduced the interaction between MARK2 and tau, and also phosphorylation of tau at Ser(262).

Related Edges 5

• a(CHEBI:staurosporine) decreases act(p(HGNC:MARK2), ma(kin))
• p(FPLX:"CAMK2_complex") increases p(HGNC:MAPT, pmod(Ph, Ser, 262))
• act(p(FPLX:PKA), ma(kin)) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 262))
• p(HGNC:CHEK2) increases p(HGNC:MAPT, pmod(Ph, Ser, 262))
• act(p(HGNC:MARK2), ma(kin)) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 262))

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