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Oncogenic KRAS mutations modulate BAX-mediated cell death.

Anabela Ferreira1, Stéphen Manon2, Akandé Rouchidane Eyitayo2

  • 1Centre of Molecular and Environmental Biology (CBMA), Department of Biology, Campus de Gualtar, University of Minho, 4710-057 Braga, Portugal; Institute of Science and Innovation for Bio-Sustainability (IB-S), Campus de Gualtar, University of Minho, 4710-057 Braga, Portugal.

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Summary
This summary is machine-generated.

Mutated Kirsten rat sarcoma viral oncogene homolog (KRAS) in colorectal cancer (CRC) confers resistance to cell death by directly interacting with the pro-apoptotic protein BAX. This interaction affects BAX-induced cell death and cytochrome c release.

Keywords:
BAXColorectal cancerHumanized yeastKRASOncogenic mutations

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncology

Background:

  • Kirsten rat sarcoma viral oncogene homolog (KRAS) is a GTPase involved in cell signaling and apoptosis.
  • Oncogenic KRAS mutations are prevalent in 30-50% of colorectal cancer (CRC) patients.
  • The role of KRAS mutations in apoptosis regulation, particularly concerning BAX, is not well understood.

Purpose of the Study:

  • To investigate the role of mutated human KRAS in regulating BAX, a key pro-apoptotic protein.
  • To elucidate the interaction between KRAS isoforms and BAX.
  • To explore the effect of acetic acid on cell death in the context of KRAS mutations and BAX.

Main Methods:

  • Utilized the yeast model Saccharomyces cerevisiae.
  • Co-expressed wild-type KRAS (KRASWT) or common CRC KRAS mutants (KRASG12D, KRASG12V, KRASG13D) with human BAX in yeast cells lacking the ras2 isoform.
  • Assessed cell death, cytochrome c release, and protein co-localization at mitochondria.

Main Results:

  • KRAS mutants, unlike KRASWT, conferred resistance to BAX-induced cell death and cytochrome c release.
  • Evidence suggests direct interaction and mitochondrial co-localization between KRAS isoforms and BAX.
  • Acetic acid significantly increased cell death in cells expressing BAX and oncogenic KRAS mutants, but not KRASWT.

Conclusions:

  • Mutated KRAS directly modulates BAX function, leading to resistance to apoptosis.
  • The findings suggest a direct physical interaction between KRAS and BAX at the mitochondria.
  • Oncogenic KRAS mutations may sensitize cancer cells to acetate, offering potential therapeutic insights.