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Updated: Jun 29, 2025

Studying TGF-β Signaling and TGF-β-induced Epithelial-to-mesenchymal Transition in Breast Cancer and Normal Cells
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Transmembrane protein 25 abrogates monomeric EGFR-driven STAT3 activation in triple-negative breast cancer

Chakrabhavi Dhananjaya Mohan1, Kanchugarakoppal S Rangappa2, Gautam Sethi3

  • 1FEST Division CSIR-Indian Institute of Toxicology Research Lucknow Uttar Pradesh India.

Medcomm
|March 27, 2024
PubMed

Insights

TMEM25 protein binds to EGFR monomers, preventing STAT3 phosphorylation in normal cells. Without TMEM25, EGFR monomers activate STAT3, impacting cellular signaling pathways.

Area of Science:

  • Cellular biology
  • Molecular signaling

Background:

  • Epidermal Growth Factor Receptor (EGFR) signaling is crucial for cell growth and survival.
  • Signal transducer and activator of transcription 3 (STAT3) is a key transcription factor involved in various cellular processes.

Purpose of the Study:

  • To investigate the role of TMEM25 in regulating EGFR signaling.
  • To elucidate the mechanism by which TMEM25 affects STAT3 phosphorylation.

Main Methods:

  • Co-immunoprecipitation assays to assess protein-protein interactions.
  • Western blotting to analyze protein phosphorylation levels.

Main Results:

  • TMEM25 physically associates with EGFR monomers in wild-type cells.
  • TMEM25 suppresses EGFR-mediated STAT3 phosphorylation.
  • Absence of TMEM25 leads to basal-level STAT3 phosphorylation by EGFR monomers.

Conclusions:

  • TMEM25 acts as a negative regulator of EGFR signaling by inhibiting STAT3 phosphorylation.
  • TMEM25 is essential for maintaining the cytoplasmic sequestration of unphosphorylated STAT3.

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