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Expanding the PP2A Interactome by Defining a B56-Specific SLiM.

Xinru Wang1, Rakhi Bajaj1, Mathieu Bollen2

  • 1Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912, USA.

Structure (London, England : 1993)
|December 22, 2016
PubMed
Summary

Researchers uncovered how short linear motifs (SLiMs) bind to protein phosphatase 2A (PP2A), a key cancer target. This discovery enables identification of PP2A regulators and substrates for disease treatment.

Keywords:
B56BubR1NMR spectroscopyPP2ARepoManX-ray crystallographymitosisphosphorylationsmall linear motif (SLiM)

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Protein-protein interactions mediated by short linear motifs (SLiMs) are crucial for cellular signaling.
  • Serine/threonine phosphatases (PSPs), including PP1, PP2A, and PP2B/calcineurin, utilize SLiMs to recruit substrates and regulators.
  • While SLiM interactions with PP1 and PP2B are well-studied, the binding mechanisms for PP2A, a cancer drug target, remain largely unknown.

Purpose of the Study:

  • To elucidate the structural basis of SLiM interactions with protein phosphatase 2A (PP2A).
  • To identify the specific SLiM motif recognized by PP2A.
  • To leverage structural insights for discovering novel PP2A regulators and substrates.

Main Methods:

  • Determined three crystal structures of PP2A-SLiM complexes (B56:pS-RepoMan, B56:pS-BubR1, B56:pSpS-BubR1).
  • Defined the consensus sequence for PP2A-specific SLiMs.
  • Utilized structural data to predict and identify new PP2A-interacting proteins.

Main Results:

  • Provided the first structural insights into how SLiMs bind to PP2A.
  • Identified and characterized the LSPIxE motif as specific for PP2A SLiM interactions.
  • Discovered numerous potential PP2A regulators and substrates based on the LSPIxE motif.

Conclusions:

  • The LSPIxE motif is a key determinant for PP2A SLiM recognition.
  • Structural understanding of PP2A-SLiM interactions facilitates the dissection of PP2A regulatory networks.
  • These findings offer a powerful strategy for targeting PP2A in diseases like cancer.