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A PDZ-kinase allosteric relay mediates Par complex regulator exchange.

Elizabeth Vargas1, Rhiannon R Penkert1, Kenneth E Prehoda1

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The Par complex, crucial for cell polarization, involves atypical Protein Kinase C (aPKC), Cdc42, and Par-3. This study reveals an allosteric relay mechanism connecting Cdc42 and Par-3 binding, explaining Par complex activity.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Par complex regulates cell polarity in animal cells through atypical Protein Kinase C (aPKC).
  • Cdc42 and Par-3 are upstream regulators that bind separately to the Par complex, influencing its activity.
  • The distinct binding sites of Cdc42 and Par-3 raise questions about their cross-regulation.

Purpose of the Study:

  • To investigate the regulatory interplay between Cdc42, Par-3, and the Par complex.
  • To elucidate the mechanism by which Par-3 binding to aPKC is modulated.
  • To understand how these interactions contribute to Par complex-mediated cell polarization.

Main Methods:

  • Biochemical assays to study protein interactions.
  • Analysis of autoinhibition mechanisms within aPKC.
  • Investigating the role of the Par-6 PDZ domain in regulating aPKC activity.

Main Results:

  • Par-3 binding to aPKC is regulated by aPKC autoinhibition.
  • The Par-6 PDZ domain activates aPKC binding to Par-3 through a novel interaction with the aPKC kinase domain.
  • Cdc42 and Par-3 exert opposing effects on the Par-6 PDZ-aPKC kinase interaction, establishing an allosteric relay.

Conclusions:

  • An allosteric relay mechanism connects Cdc42 and Par-3 binding sites within the Par complex.
  • This relay, involving differential effects on the Par-6 PDZ-aPKC kinase interaction, underlies the negative cooperativity essential for Par complex polarization and activity.