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Regulation of NF-kB Signalling Through the PR55β-RelA Interaction in Osteoblasts

Azusa Suzuki1, Goro Sugiyama2, Yukiko Ohyama1

  • 1Section of Oral and Maxillofacial Surgery, Division of Maxillofacial Diagnostic and Surgical Sciences, Faculty of Dental Science, Kyushu University, Fukuoka, Japan.

In Vivo (Athens, Greece)
|March 1, 2020
PubMed
Abstract

Insights

Fibroblast growth factor 2 (FGF2) stimulation increases PR55β expression, which dephosphorylates and regulates nuclear factor kappa B (NF-kB) signaling via RelA interaction.

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Biochemistry

Background:

  • Nuclear factor kappa B (NF-kB) signaling, including the RelA subunit, is activated by fibroblast growth factor (FGF).
  • Protein phosphatase 2A (PP2A) is implicated in RelA dephosphorylation, but the precise mechanism remains unclear.
  • Understanding these mechanisms offers insights for molecular targeting therapies.

Purpose of the Study:

  • To investigate the role of PP2A regulatory subunits in NF-kB signaling.
  • To elucidate the interaction between FGF2, PP2A, and the RelA subunit.
  • To clarify the mechanism of RelA dephosphorylation upon FGF stimulation.

Main Methods:

  • Quantitative reverse transcription PCR (qRT-PCR) and immunoblot analysis to assess subunit expression in MC3T3-E1 cells.
  • Immunocytochemistry (IC), immunoprecipitation (IP), and pull-down assays (PD) to examine FGF2-NF-kB interactions.
  • Use of recombinant proteins in interaction assays.

Main Results:

  • FGF2 stimulation led to increased PR55β expression.
  • Activated RelA was dephosphorylated following FGF2 stimulation.
  • Direct interaction between PR55β and RelA was confirmed via IC, IP, and PD.

Conclusions:

  • FGF2-induced PR55β directly interacts with the RelA subunit.
  • This interaction plays a regulatory role in FGF2-mediated NF-kB signaling.
Keywords:
FGF2NF-kBPP2APR55βRelAosteoblast

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