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Tau and GSK3β Dephosphorylations are Required for Regulating Pin1 Phosphorylation

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Pin1 binds mitotically phosphorylated Thr231–Pro232 and Thr212–Pro213 sites on tau, and a Pin1 deficiency in mice leads to tau hyperphosphorylation. The aim of this study was to determine if the dephosphorylation or inhibition of tau and GSK3β phosphorylation induces the Pin1 phosphorylation. To test this, human SK-N-MC cells were stably transfected with a fusion gene containing neuron-specific enolase (NSE)-controlled APPsw gene(NSE/APPsw), to induce Aβ-42. The stable transfectants were then transiently transfected with NSE/Splice, lacking human tau (NSE/Splice), or NSE/hTau, containing human tau, into the cells. The NSE/Splice- and NSE/hTau-cells were then treated with lithium. We concluded that (i) there was more C99-β APP accumulation than C83-βAPP in APPsw-tansfectant and thereby promoted Aβ-42 production in transfectants. (ii) the inhibition of tau and GSK3β phosphorylations correlated with increase in Pin1 activation in NSE/hTau- cells. Thus, these observations suggest that Pin1 might have an inhibitive role in phosphorylating tau and GSK3β for protecting against Alzheimer’s disease.

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Authors and Affiliations

  1. Division of Laboratory Animal Resources, National Institute of Toxicological Research, Korea FDA, 122-704, Seoul, Korea

    Sae H. Min, Jung S. Cho, Jae H. Oh, Sun B. Shim, Dae Y. Hwang, Su H. Lee, Seung W. Jee, Hwa J. Lim, Min Y. Kim, Seok H. Lee & Yong K. Kim

  2. College of Pharmacy, Ewha Womans University, 122-150, Seoul, Korea

    Yhun Y. Sheen

  3. Division of Laboratory Laboratory Resources, National Institute of Toxicological Research, Korea FDA, 5 Nokbundong Eunpyungku, 122-704, Seoul, Korea

    Yong K. Kim

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  1. Sae H. Min
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Correspondence to Yong K. Kim.

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Min, S.H., Cho, J.S., Oh, J.H. et al. Tau and GSK3β Dephosphorylations are Required for Regulating Pin1 Phosphorylation. Neurochem Res 30, 955–961 (2005). https://doi.org/10.1007/s11064-005-6177-0

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