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ASPPs multimerize protein phosphatase 1.

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  • 1Department of Molecular Medicine, Cornell University, Ithaca, New York, United States of America.

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|October 16, 2025
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Summary
This summary is machine-generated.

Ankyrin repeat, SH3-domain, and Proline-rich region containing Proteins (ASPPs) bind Protein Phosphatase 1 (PP1) and multimerize it. This creates concentrated phosphatase hubs at cell junctions, a mechanism revealed by genetic studies in C. elegans.

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Protein Phosphatase 1 (PP1) activity is regulated by numerous subunits, but their functions are unclear.
  • Ankyrin repeat, SH3-domain, and Proline-rich region containing Proteins (ASPPs) are known to bind and localize PP1 to cell-cell junctions.

Purpose of the Study:

  • To investigate the mechanism by which ASPPs regulate PP1 activity at cell-cell junctions.
  • To elucidate the role of ASPP ankyrin repeats in PP1 binding and stoichiometry.

Main Methods:

  • Biochemical assays to determine PP1 binding stoichiometry with ASPPs.
  • Analysis of missense mutations in ASPP ankyrin repeats identified through genetic screening in Caenorhabditis elegans.
  • In vivo functional assays to assess the impact of PP1 oligomerization on mutant ASPP function.

Main Results:

  • ASPPs bind superstoichiometric amounts of PP1.
  • Specific missense mutations in ASPP ankyrin repeats decrease PP1 binding stoichiometry.
  • Restoring PP1 oligomerization rescues the function of mutant ASPPs in vivo.

Conclusions:

  • ASPPs function by multimerizing PP1, creating concentrated hubs of phosphatase activity at cell-cell junctions.
  • The ankyrin repeat domain of ASPPs is critical for high-stoichiometry PP1 binding and subsequent PP1 multimerization.