p(HGNC:GSK3B) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 404))

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PubMed:14612456

These data indicated that phosphorylation of PP2A dephosphorylation sites is an important recognition signal for ubiquitination. We used 200 μg of amino-terminal His-tagged full-length recombinant human tau in an in vitro phosphorylation reaction with GSK-3Beta. When phosphorylated, the tau protein reacted on immunoblots with PHF1 (25, 26) and AT8 (24), indicating that at least sites Ser202, Thr205, Ser396, and Ser404 were phosphorylated. Following GSK-3Beta incubation, this tau served as an excellent substrate for in vitro ubiquitination using UbcH5B and the cofactor fraction from AD tau immunoprecipitates (Fig. 2a). This finding suggested that GSK-3Beta can place phosphates on tau that create recognition sites for an E3 Ub ligase.

Related Edges 5

• p(HGNC:GSK3B) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 202))
• p(HGNC:GSK3B) directlyIncreases p(HGNC:MAPT, pmod(Ph, Thr, 205))
• p(HGNC:GSK3B) directlyIncreases p(HGNC:MAPT, pmod(Ph, Ser, 396))
• p(HGNC:MAPT, pmod(Ph)) positiveCorrelation p(HGNC:MAPT, pmod(Ub))
• p(HGNC:MAPT, pmod(Ub)) positiveCorrelation p(HGNC:MAPT, pmod(Ph))

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