PubMed: 10464280

Title
Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies.
Journal
The Journal of biological chemistry
Volume
274
Issue
None
Pages
25490-8
Date
1999-09-03
Authors
Brandt R | Bloom GS | Kuret J | Sontag E | Kamibayashi C | White CL 3rd | Lee G | Nunbhakdi-Craig V | Mumby MC

Evidence 1b9297df0a

ABaC binds directly to MTs through a site that encompasses its catalytic subunit and is distinct from its binding site for tau, and ABaC and tau bind to different domains on MTs.

Evidence 802c02b002

Using tau deletion mutants, we found that ABaC binds a domain on tau that is indistinguishable from its MT-binding domain.

Evidence 71ed5b1923

Thus, MTs inhibited the rate of tau dephosphorylation by ABaC.

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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.