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Ndr/Lats Kinases Bind Specific Mob-Family Coactivators through a Conserved and Modular Interface.

Benjamin W Parker1, Gergo Gogl2,3, Mónika Bálint4

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Ndr/Lats kinases and Mob cofactors form essential Hippo pathway complexes. Structural analysis reveals how Mob proteins organize kinase regulation, with specific binding sites determining cofactor specificity.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Hippo signaling pathways regulate cell proliferation and morphogenesis.
  • Ndr/Lats kinases bind Mob coactivator proteins, forming essential complexes.
  • Ndr/Lats kinases possess an N-terminal regulatory (NTR) region crucial for Mob cofactor interaction.

Purpose of the Study:

  • To elucidate the structural basis of Ndr/Lats kinase-Mob cofactor association and specificity.
  • To understand the regulatory mechanism mediated by the Ndr/Lats NTR-Mob interface.
  • To identify the determinants of selective binding between Ndr/Lats kinases and distinct Mob cofactors.

Main Methods:

  • Determined crystal structures of Saccharomyces cerevisiae Cbk1NTR-Mob2 and Dbf2NTR-Mob1 complexes.
  • Experimentally assessed determinants of Mob cofactor binding and specificity.
  • Analyzed the Ndr/LatsNTR-Mob interface and its interaction with the AGC kinase C-terminal hydrophobic motif (HM).

Main Results:

  • The Ndr/LatsNTR-Mob interface organizes the NTR to interact with the AGC kinase HM for allosteric regulation.
  • The Mob-organized NTR mediates HM association with an allosteric site on the N-terminal kinase lobe.
  • Cofactor specificity is determined by discrete sites within the Ndr/Lats NTR, as demonstrated by altering residues to allow noncognate Mob binding.

Conclusions:

  • The Ndr/LatsNTR-Mob interface is a common structural platform for kinase-cofactor binding.
  • Mob cofactors play a critical role in organizing Ndr/Lats kinase regulation via the NTR.
  • Specific binding sites within the NTR dictate cofactor specificity, providing a mechanism for pathway regulation.