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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

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The serine/threonine phosphatase PPM1B (PP2Cβ) selectively modulates PPARγ activity.

Ismayil Tasdelen¹, Olivier van Beekum, Olena Gorbenko

¹Department of Metabolic Diseases, University Medical Centre Utrecht, Utrecht, The Netherlands.

The Biochemical Journal

|January 17, 2013

Summary

The protein phosphatase PPM1B dephosphorylates and selectively modulates the activity of the nuclear receptor PPARγ. This interaction occurs in the nucleus and affects PPARγ-mediated gene expression in adipocytes.

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Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

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Published on: July 17, 2020

Area of Science:

Molecular Biology
Cellular Regulation
Biochemistry

Background:

Reversible protein phosphorylation regulates transcription factors like PPARγ.
Phosphorylation at Ser(112) and Ser(273) alters PPARγ transcriptional activity.
Few enzymes are known to dephosphorylate nuclear receptors.

Purpose of the Study:

To identify novel proteins that regulate PPARγ.
To investigate the role of identified proteins in PPARγ dephosphorylation and activity.

Main Methods:

Immunoprecipitation assays.
Tandem mass spectrometry (MS) analysis.
Cellular knockdown experiments in 3T3-L1 adipocytes.

Main Results:

Identified PPM1B (protein phosphatase, Mg(2+)/Mn(2+) dependent, 1B) as a PPARγ-interacting protein.
Demonstrated PPM1B dephosphorylates PPARγ in vitro and in intact cells.
Showed PPM1B enhances PPARγ-mediated transcription via Ser(112) dephosphorylation.
Observed PPM1B knockdown selectively alters PPARγ target gene expression.

Conclusions:

PPM1B is a novel nuclear phosphatase that interacts with PPARγ.
PPM1B directly dephosphorylates PPARγ, enhancing its transcriptional activity.
PPM1B acts as a selective modulator of PPARγ activity.