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Assay for Three-Way Interaction of Protein Phosphatase-1 (Glc7) With Regulatory Subunits Plus Phosphatase Inhibitor-2

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Book cover Protein Phosphatase Protocols

Part of the book series: Methods in Molecular Biology ((MIMB,volume 365))

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Abstract

A method is described using yeast conjugation to assay the interactions of a protein phosphatase-1 (PP1) inhibitor protein with holoenzymes formed in situ by expression of regulatory subunit fusion proteins that recruit endogenous Glc7, the yeast ortholog of PP1. Mutations in the canonical recognition motif VxF used to bind PP1 (Glc7) allow for analysis of direct from indirect (three-way) interactions.

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Author information

Authors and Affiliations

  1. Department of Physiology, Thomas Jefferson College of Medicine, Philadelphia, Pennsylvania, USA

    Masumi Eto

  2. Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia, USA

    David L. Brautigan

  3. Department of Microbiology, University of Virginia School of Medicine, Charlottesville, Virginia, USA

    David L. Brautigan

Authors
  1. Masumi Eto
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  2. David L. Brautigan
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Editor information

Editors and Affiliations

  1. Department of Biological Sciences, University of Calgary, Calgary, Alberta, Canada

    Greg Moorhead

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© 2007 Humana Press Inc.

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Eto, M., Brautigan, D.L. (2007). Assay for Three-Way Interaction of Protein Phosphatase-1 (Glc7) With Regulatory Subunits Plus Phosphatase Inhibitor-2. In: Moorhead, G. (eds) Protein Phosphatase Protocols. Methods in Molecular Biology, vol 365. Springer, Totowa, NJ. https://doi.org/10.1385/1-59745-267-X:197

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  • DOI: https://doi.org/10.1385/1-59745-267-X:197

  • Publisher Name: Springer, Totowa, NJ

  • Print ISBN: 978-1-58829-711-2

  • Online ISBN: 978-1-59745-267-0

  • eBook Packages: Springer Protocols

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