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Related Experiment Video

Updated: Aug 7, 2025

Monitoring Hippo Signaling Pathway Activity Using a Luciferase-based Large Tumor Suppressor LATS Biosensor
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Phosphorylation-linked complex profiling identifies assemblies required for Hippo signal integration.

Federico Uliana1,2, Rodolfo Ciuffa1, Ranjan Mishra2

  • 1Department of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.

Molecular Systems Biology
|March 10, 2023
PubMed
Summary
This summary is machine-generated.

This study introduces a new experimental method to link protein phosphorylation sites with protein-protein interactions (PPIs). The approach was used to study YAP1, revealing how its phosphorylation and complex formation are regulated by the Hippo pathway.

Keywords:
Interaction proteomicsProtein phosphorylationProtein-protein interactionsYAP1

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Predicting functional relevance of phosphorylation sites computationally is established.
  • Experimental analysis of the interplay between protein phosphorylation and protein-protein interactions (PPIs) is challenging.
  • Understanding these interdependencies is crucial for deciphering cellular signaling networks.

Purpose of the Study:

  • To develop and validate an experimental strategy for investigating the interdependencies between protein phosphorylation and protein complex formation.
  • To apply this strategy to YAP1, a key regulator of organ size and tissue homeostasis.
  • To elucidate how Hippo pathway signaling controls YAP1 phosphorylation and its association with different protein complexes.

Main Methods:

  • Systematic charting of a target protein's phosphorylation landscape.
  • Native complex separation (AP-BNPAGE) and protein correlation profiling to assign proteoforms to specific complexes.
  • Analysis of proteoforms and complexes in cells with altered expression of key regulatory proteins.

Main Results:

  • Identified multiple YAP1 phosphosites linked to distinct protein complexes.
  • Inferred the regulatory roles of Hippo pathway members on YAP1 phosphorylation and complex formation.
  • Detected a PTPN14/LATS1/YAP1 complex and proposed a model for PTPN14-mediated inhibition of YAP1.

Conclusions:

  • The developed strategy effectively establishes interdependencies between protein phosphorylation and complex formation.
  • Hippo pathway signaling dynamically regulates YAP1 phosphorylation and its interaction partners.
  • PTPN14 may inhibit YAP1 activity through enhanced complex formation and LATS1/2-mediated phosphorylation.