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Regulation of PTP1B activation through disruption of redox-complex formation

Avinash D Londhe1, Alexandre Bergeron2,3, Stephanie M Curley1

  • 1Department of Nanobioscience, College of Nanoscale Science and Engineering, SUNY Polytechnic Institute, Albany, NY, USA.

Nature Chemical Biology
|December 25, 2019
PubMed

Insights

Researchers found that blocking the interaction between protein tyrosine phosphatase 1B (PTP1B) and 14-3-3ζ prevents PTP1B inactivation and may offer a way to activate PTP1B in cells.

Area of Science:

  • Molecular biology
  • Cell signaling
  • Enzymology

Background:

  • Protein tyrosine phosphatase 1B (PTP1B) is a key regulator of cellular signaling pathways.
  • PTP1B activity is modulated by post-translational modifications, including reversible oxidation.
  • 14-3-3 proteins are known to interact with and regulate various signaling molecules.

Purpose of the Study:

  • To investigate the molecular interaction between PTP1B and 14-3-3ζ.
  • To determine the role of this interaction in regulating PTP1B activity.
  • To explore the potential of modulating this interaction for therapeutic purposes.

Main Methods:

  • Biochemical assays to detect and characterize the PTP1B-14-3-3ζ interaction.
  • Cell-based experiments to assess the impact of disrupting the interaction on PTP1B activity and downstream signaling.
  • Measurement of epidermal growth factor receptor (EGFR) phosphorylation levels.

Main Results:

  • A novel molecular interaction was identified between the reversibly oxidized form of PTP1B and 14-3-3ζ.
  • Destabilizing this transient interaction prevented PTP1B inactivation by reactive oxygen species.
  • Disruption of the interaction led to decreased epidermal growth factor receptor phosphorylation.

Conclusions:

  • The interaction between 14-3-3ζ and oxidized PTP1B is crucial for PTP1B inactivation.
  • Modulating this interaction offers a potential strategy for controlling PTP1B activity.
  • Targeting the PTP1B-14-3-3ζ interaction may provide a novel therapeutic approach for diseases involving PTP1B dysregulation.

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