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Yorkie-Warts Complexes are an Ensemble of Interconverting Conformers Formed by Multivalent Interactions.

Kasie Baker1, Ethiene Kwok1, Patrick Reardon1

  • 1Department of Biochemistry & Biophysics, Oregon State University, Corvallis, OR 97331, USA.

Journal of Molecular Biology
|December 31, 2020
PubMed
Summary

Multivalent protein interactions involving Yorkie (Yki) WW domains and Warts (Wts) PPXY motifs form adaptable complexes. These assemblies, crucial for cell cycle regulation, involve tandem WW domains binding adjacent PPXY motifs, creating diverse molecular structures.

Keywords:
Hippo signaling pathwayPPXY motifWW domainintrinsically disordered proteinprotein-protein interaction

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Area of Science:

  • Molecular and Cellular Biology
  • Protein-Protein Interactions
  • Biophysics

Background:

  • Proteins with multiple WW domains and PPXY motifs are key regulators in the cell cycle.
  • The molecular mechanisms of these multivalent WW domain-PPXY assemblies are not well understood.
  • Previous studies focused on single WW domain-PPXY motif interactions.

Purpose of the Study:

  • To investigate the molecular mechanisms of multivalent WW domain-PPXY assemblies.
  • To characterize the interaction between the Yorkie (Yki) transcription coactivator and the Warts (Wts) tumor suppressor proteins.
  • To understand how these interactions contribute to cellular processes.

Main Methods:

  • Isothermal titration calorimetry (ITC).
  • Sedimentation velocity analytical ultracentrifugation (SV-AUC).
  • Size-exclusion chromatography coupled to multi-angle light scattering (SEC-MALS).
  • Native-state mass spectrometry (MS).

Main Results:

  • Yorkie WW domains and Warts PPXY motifs assemble into a dynamic ensemble of complexes with variable stoichiometries.
  • Tandem WW domains bind to adjacent PPXY motifs, with additional WW domains binding to unoccupied motifs.
  • The binding involves preferential targeting of C-terminal PPXY motifs on Warts.

Conclusions:

  • Multivalent WW domain-PPXY interactions form interconverting complexes, not just simple one-to-one binding.
  • This complex assembly mechanism enhances the adaptability and versatility of WW domain-PPXY-mediated cellular processes.
  • Such dynamic assemblies may be a common strategy for intricate cellular regulation.