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. 2013 Jan 28;288(11):7968–7977. doi: 10.1074/jbc.M112.433326

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© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 2. — Recombinant Tau phosphorylated in vitro by Cdk5-p25 or GSK3β, but not by PKA, binds to Pin1. A, recombinant Tau phosphorylated by Cdk5-p25, GSK3β, or PKA was subjected to a GST-Pin1 pulldown assay. s, supernatant; p, pellet. Unphosphorylated Tau is shown in the first panel ([−]). Tau bound to GST-Pin1 was detected by immunoblotting with Tau5 (first to fourth panels). The input is shown in the lanes labeled “In.” GST-Pin1 and GST are shown by CBB staining (lower panel). B, Tau binds to Pin1 at phosphorylation sites other than Thr-212 and Thr-231. Tau-T212A, Tau-T231A, or Tau-T212A/T231A was phosphorylated by Cdk5-p25 and subjected to the GST pulldown assay. Tau bound to Pin1 (upper panel) and in the input (second panel) was detected by immunoblotting with Tau5. CBB staining shows GST-Pin1 (lower panel). C, the WW domain-dependent binding of Pin1 to Cdk5-phosphorylated Tau. Unphosphorylated Tau (−) or Cdk5-phosphorylated Tau (Cdk5-p25) was subjected to the GST pulldown assay using an Asp mutant of Pin1 at Tyr-23 (Y23D) or Trp-34 (W34D) in the WW domain. Input shows unphosphorylated (−) and Cdk5-phosphorylated (Cdk5) Tau. CBB staining shows GST-Pin1 and GST (lower panel).