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Identification of intracellular cavin target proteins reveals cavin-PP1alpha interactions regulate apoptosis

Kerrie-Ann McMahon1, Yeping Wu1, Yann Gambin1,2

  • 1The University of Queensland, Institute for Molecular Bioscience, Brisbane, QLD, 4072, Australia.

Nature Communications
|July 24, 2019
PubMed

Insights

Cellular stress triggers cavins to leave caveolae and interact with intracellular targets. This study identifies cavin interactions with proteins like PP1α, revealing a new pro-apoptotic pathway from the cell surface to the nucleus.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Caveolae are specialized plasma membrane domains crucial for cellular functions.
  • Caveolae formation depends on Caveolin-1/3 and cavin proteins.
  • Stress induces caveolae disassembly, releasing cavins for potential intracellular interactions.

Purpose of the Study:

  • To identify intracellular cavin-binding proteins and elucidate their functions.
  • To investigate the role of cavin-protein interactions in stress signaling and apoptosis.

Main Methods:

  • Biotin affinity proteomics and mass spectrometry to identify cavin interactors.
  • Cell-free expression systems and protein-protein binding assays for validation.
  • Pathway analysis to determine functional roles of identified interactors.

Main Results:

  • Identified and validated 47 potential intracellular cavin-interactor proteins.
  • Discovered novel roles for cavins in cellular metabolism and stress response.
  • Validated the interaction between Cavin-1/3 and protein phosphatase 1 alpha (PP1α).
  • Demonstrated that UV-induced Cavin3 release from caveolae inhibits PP1α, promoting apoptosis via H2AX phosphorylation.

Conclusions:

  • Caveolae serve as a platform for stress-induced signaling pathways.
  • Cavin proteins mediate a novel pro-apoptotic signaling cascade involving PP1α inhibition.
  • This pathway links plasma membrane events to nuclear events, influencing cell fate decisions.

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