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Structural basis for the interaction between the cell polarity proteins Par3 and Par6.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cell polarity is fundamental for cell function and development.
  • The Par protein complex (aPKC, Par3, Par6) regulates asymmetric protein localization.
  • Dysfunction of the Par complex is linked to developmental abnormalities and cancer.

Purpose of the Study:

  • To investigate the interaction between Par3 and Par6.
  • To elucidate the role of a specific motif in Par6 for Par3 binding and localization.
  • To understand the structural basis of Par3-Par6 complex formation.

Main Methods:

  • In vitro binding assays.
  • Cell-based localization studies in cultured cells.
  • Structural analyses using X-ray crystallography and NMR spectroscopy.
  • Functional studies in fly embryos.

Main Results:

  • A PDZ domain-binding motif in Par6 was identified, crucial for Par3 interaction and membrane localization.
  • The motif was functionally redundant with Par3's PDZ domain in targeting Par6 to the cell cortex in vivo.
  • Structural analysis revealed that Par3's PDZ1 and PDZ3 domains bind to the Par6 motif, enabling simultaneous Par6 recruitment.

Conclusions:

  • Par3 can bind two Par6 proteins simultaneously via its PDZ1 and PDZ3 domains.
  • This multivalent interaction facilitates the assembly of polarity protein networks.
  • Understanding these interactions provides insights into cell polarity regulation and disease mechanisms.