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[PPP2R2A binds and dephosphorylates GFPT2 in breast cancer cells]

Xiaorong Li1, Jin Zhang1, Duan Ma1

  • 1School of Basic Medical Sciences, Fudan University, Shanghai 200012, China.

Sheng Wu Gong Cheng Xue Bao = Chinese Journal of Biotechnology
|June 27, 2018
PubMed

Insights

Protein phosphatase 2 regulatory subunit B alpha (PPP2R2A) interacts with GFPT1/2, impacting GFPT2 phosphorylation and O-GlcNAcylation. This discovery offers new insights into cancer cell survival and growth regulation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Protein phosphatase 2 regulatory subunit B alpha (PPP2R2A) is implicated in cancer cell survival and growth.
  • Understanding PPP2R2A's interactions is crucial for cancer research.

Purpose of the Study:

  • To identify proteins that bind to PPP2R2A.
  • To investigate the functional consequences of PPP2R2A interactions on cancer cell metabolism.

Main Methods:

  • Tandem affinity purification coupled with HPLC-Chip-ESI/MS/MS mass spectrometry.
  • GST Pull-down, co-immunoprecipitation, and immunofluorescence assays.
  • Lentivirus-mediated shRNA for gene knockdown.

Main Results:

  • GFPT1 and GFPT2 were identified as potential PPP2R2A-binding proteins.
  • Knockdown of PPP2R2A enhanced GFPT2 phosphorylation but not GFPT1.
  • PPP2R2A knockdown promoted total cellular O-GlcNAcylation in breast cancer cells.

Conclusions:

  • PPP2R2A interacts with GFPT1 and GFPT2, modulating GFPT2 phosphorylation.
  • This interaction influences cellular O-GlcNAcylation, a pathway relevant to cancer.
  • Findings suggest a novel regulatory mechanism of the hexosamine pathway in cancer cells.
Keywords:
GFPT1GFPT2O-GlcNAcylationPPP2R2A

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