Abstract
Protein phosphatase-2A (PP2A) activity, which is compromised in Alzheimer disease brain, is regulated by two endogenous inhibitors, one of them being I 2 PP2A, a 277 amino acid long protein also known as SET. Here we report that both the amino terminal fragment (I 2NTF; aa 1–175) and the carboxy terminal fragment (I 2CTF; aa 176–277) of I 2 PP2A inhibit PP2A by binding to its catalytic subunit PP2Ac and cause hyperphosphorylation of tau. The C-terminal acidic region in I 2CTF and Val 92 in I 2NTF are essential for their association with PP2Ac and inhibition of the phosphatase activity. Structured summary of protein interactions I2PP2A physically interacts with PP2A-C by anti tag coimmunoprecipitation (view interaction 1, 2) I2PP2A physically interacts with PP2A-C by pull down (view interaction 1, 2) PP2A-A physically interacts with PP2A-B and PP2A-C by pull down (view interaction)
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