Transmembrane protein 25 abrogates monomeric EGFR‐driven STAT3 activation in triple‐negative breast cancer

Transmembrane protein 25 abrogates monomeric EGFR‐driven STAT3 activation in triple‐negative breast cancer

In wild‐type cells, TMEM25 physically associates with EGFR monomer and suppresses the EGFR‐mediated STAT3 phosphorylation, which results in the sequestration of unphosphorylated STAT3 in the cytoplasm. In TMEM‐/‐ cells, EGFR monomer phosphorylates STAT3 at the basal level.

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Veröffentlicht in:MedComm 2024-04, Vol.5 (4), p.e492-n/a
Hauptverfasser: Mohan, Chakrabhavi Dhananjaya, Rangappa, Kanchugarakoppal S., Sethi, Gautam
Format: Artikel
Sprache:eng
Schlagworte:
Biomarkers
Breast cancer
Conflicts of interest
Epidermal growth factor
Glioma
Highlights
Kinases
Metastasis
Phosphorylation
Proteins
Signal transduction
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Zusammenfassung:In wild‐type cells, TMEM25 physically associates with EGFR monomer and suppresses the EGFR‐mediated STAT3 phosphorylation, which results in the sequestration of unphosphorylated STAT3 in the cytoplasm. In TMEM‐/‐ cells, EGFR monomer phosphorylates STAT3 at the basal level.
ISSN:2688-2663
2688-2663
DOI:10.1002/mco2.492