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Regulation of GSK3 isoforms by phosphatases PP1 and PP2A

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Abstract

Dephosphorylation of phospho GSK3 isoforms, from COS-7 cells, was determined in vitro and in cultured cells in the absence or the presence of okadaic acid and lithium. Our results indicate a preferential dephosphorylation of phospho GSK3α by PP2A phosphatase, whereas dephosphorylation of phospho GSK3β mainly takes place by PP1 phosphatase.

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Acknowledgments

This study was supported by grants from the Comunidad de Madrid (NEURODEGMODELS-CM), the Spanish Comisión Interministerial de Ciencia y Tecnologia, Fundación Centro Investigación Enfermedades Neurológicas (Fundación CIEN), and the CIBER on Neurodegeneration and by institutional grants from the Fundación Ramón Areces.

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Authors and Affiliations

  1. Centro de Biologia Molecular “Severo Ochoa” (CSIC-UAM), Campus de Cantoblanco, 28049, Madrid, Spain

    Félix Hernández, Elena Langa, Raquel Cuadros & Jesús Avila

  2. CIBERNED, 28031, Madrid, Spain

    Jesús Avila

  3. Centro Nacional de Microbiología, Instituto de Salud Carlos III, Ctra. Majadahonda, 28220, Madrid, Spain

    Nieves Villanueva

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  1. Félix Hernández
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  2. Elena Langa
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  3. Raquel Cuadros
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  4. Jesús Avila
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  5. Nieves Villanueva
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Correspondence to Jesús Avila.

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Hernández, F., Langa, E., Cuadros, R. et al. Regulation of GSK3 isoforms by phosphatases PP1 and PP2A. Mol Cell Biochem 344, 211–215 (2010). https://doi.org/10.1007/s11010-010-0544-0

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  • DOI: https://doi.org/10.1007/s11010-010-0544-0

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