Hippo pathway controls biopterin metabolism to shield adjacent cells from ferroptosis in lung cancer

EMBO Rep. 2025 Aug;26(16):4124-4152. doi: 10.1038/s44319-025-00515-4. Epub 2025 Jul 7.

Abstract

Recent advances in single-cell technologies have uncovered significant cellular diversity in tumors, influencing cancer progression and treatment outcomes. The Hippo pathway controls cell proliferation through its downstream effectors: yes-associated protein (YAP) and transcriptional co-activator with PDZ-binding motif (TAZ). Our analysis of human lung adenocarcinoma and murine models revealed that cancer cells display heterogeneous YAP/TAZ activation levels within tumors. Murine lung cancer cells with high YAP/TAZ activity grow rapidly but are sensitive to ferroptosis, a cell death induced by lipid peroxidation. In contrast, cells with low YAP/TAZ activity grow slowly but resist ferroptosis. Moreover, they protect neighbouring cells from ferroptosis, creating a protective microenvironment that enhances the tumor's resistance to ferroptosis. Mechanistically, inhibiting YAP/TAZ upregulates GTP cyclohydrolase 1 (GCH1), an enzyme critical for the biosynthesis of tetrahydrobiopterin (BH4), which functions as a secretory antioxidant to prevent lipid peroxidation. Pharmacological inhibition of GCH1 sensitizes lung cancer cells to ferroptosis inducers, suggesting a potential therapeutic approach. Our data highlights the non-cell-autonomous roles of the Hippo pathway in creating a ferroptosis-resistant tumor microenvironment.

Keywords: Biopterin; Cell Communication; Ferroptosis; Hippo Pathway; Lung Cancer.

MeSH terms

  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism
  • Animals
  • Biopterins* / analogs & derivatives
  • Biopterins* / metabolism
  • Cell Line, Tumor
  • Cell Proliferation
  • Ferroptosis*
  • Hippo Signaling Pathway
  • Humans
  • Lipid Peroxidation
  • Lung Neoplasms* / genetics
  • Lung Neoplasms* / metabolism
  • Lung Neoplasms* / pathology
  • Mice
  • Protein Serine-Threonine Kinases* / metabolism
  • Signal Transduction*
  • Transcription Factors / metabolism
  • Tumor Microenvironment
  • YAP-Signaling Proteins

Substances

  • Biopterins
  • Protein Serine-Threonine Kinases
  • YAP-Signaling Proteins
  • Transcription Factors
  • Adaptor Proteins, Signal Transducing
  • sapropterin