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Trihydrophobin 1 phosphorylation by c-Src regulates MAPK/ERK signaling and cell migration

Weibin Wu1, Zhichao Sun, Jingwen Wu

  • 1Gene Research Center, Shanghai Medical College, Fudan University, Shanghai, China.

Plos One
|January 13, 2012
PubMed

Insights

c-Src phosphorylation of trihydrophobin 1 (TH1) disrupts its interaction with A-Raf and PAK1. This reduces TH1

Area of Science:

  • Cell biology
  • Molecular signaling
  • Cancer research

Background:

  • c-Src kinase activates the Ras-MAPK/ERK pathway, promoting cell migration.
  • Trihydrophobin 1 (TH1) inhibits MAPK/ERK and cell migration by interacting with A-Raf and PAK1.

Purpose of the Study:

  • To investigate the interaction between c-Src and TH1.
  • To elucidate the role of TH1 phosphorylation in regulating MAPK/ERK signaling and cell migration.

Main Methods:

  • GST-pull down assay
  • Coimmunoprecipitation
  • Confocal microscopy
  • In vitro and in vivo phosphorylation assays

Main Results:

  • c-Src directly interacts with TH1.
  • c-Src phosphorylates TH1 at Tyr-6, reducing its binding to A-Raf and PAK1.
  • TH1 phosphorylation diminishes its inhibitory effect on MAPK/ERK signaling, enhancing c-Src-mediated cell migration.
  • EGF and estrogen treatments induce TH1 tyrosine phosphorylation.

Conclusions:

  • Tyrosine phosphorylation of TH1 by c-Src is a novel regulatory mechanism for Ras/Raf/MEK/ERK signaling.
  • This phosphorylation modulates TH1's interaction with A-Raf and PAK1, impacting cell migration.
  • The findings reveal a new pathway for controlling cell signaling and migration.

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