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Dephosphorylation of Girdin by PP2A inhibits breast cancer metastasis

Jiang Li1, Atsushi Enomoto2, Liang Weng3

  • 1Center for Molecular Medicine, Xiangya Hospital, Central South University, 87 Xiangya Road, 410008, Changsha, Hunan, China.

Biochemical and Biophysical Research Communications
|April 3, 2019
PubMed

Insights

Protein phosphatase 2A (PP2A) dephosphorylates Girdin, inhibiting breast cancer cell migration. Low PP2A expression correlates with advanced tumor stage and metastasis, highlighting a key pathway in cancer progression.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cell Biology

Background:

  • Girdin dysfunction is implicated in various tumors.
  • Girdin phosphorylation is well-studied, but its dephosphorylation mechanism is unknown.

Purpose of the Study:

  • To elucidate the mechanism of Girdin dephosphorylation.
  • To investigate the role of Girdin dephosphorylation in breast cancer cell migration.

Main Methods:

  • Investigated the interaction between protein phosphatase 2A (PP2A) and Girdin.
  • Utilized overexpression and knockdown of PP2A to study Girdin phosphorylation at serine 1416.
  • Analyzed human breast cancer samples for PP2A expression and Girdin phosphorylation correlation.

Main Results:

  • PP2A binds to Girdin via its B subunit.
  • PP2A regulates Girdin dephosphorylation at serine 1416.
  • PP2A-mediated Girdin dephosphorylation inhibits breast cancer cell migration.
  • PP2A expression inversely correlates with Girdin phosphorylation in human breast cancer.
  • Low PP2A expression is linked to advanced tumor stage, grade, and lymph node metastasis.

Conclusions:

  • PP2A-mediated Girdin dephosphorylation is a critical pathway regulating breast cancer cell migration.
  • PP2A represents a potential therapeutic target for breast cancer metastasis.
Keywords:
Breast cancerGirdinMigrationPP2A

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