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Phosphofructokinases Axis Controls Glucose-Dependent mTORC1 Activation Driven by E2F1.

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Glucose fuels cancer growth by activating mTORC1. This study reveals E2F1 links glucose metabolism to mTORC1 activation via lysosomal PFKFB3, offering new therapeutic targets for cancer.

Keywords:
Cell BiologyMolecular Genetics

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Area of Science:

  • Cell Biology
  • Cancer Metabolism
  • Molecular Oncology

Background:

  • Cancer cells require mTORC1 signaling for growth, linking nutrient availability with mitogenic signals.
  • The transcription factor E2F1 plays a role in cellular metabolism.
  • The interplay between E2F1, glucose metabolism, and mTORC1 activation is not fully understood.

Purpose of the Study:

  • To investigate the hypothesis that E2F1-driven glucose catabolism contributes to mTORC1 activation.
  • To elucidate the role of glucose in E2F1-mediated mTORC1 activation.
  • To identify key molecular players in this signaling pathway.

Main Methods:

  • Cellular assays to measure mTORC1 activity and translocation.
  • Analysis of E2F1-regulated gene expression, focusing on glycolytic enzymes.
  • Biochemical methods to assess enzyme activity and protein-protein interactions at the lysosome.

Main Results:

  • Glucose enhances E2F1-induced mTORC1 activation by promoting its lysosomal translocation, independent of AMPK.
  • E2F1 upregulates aerobic glycolysis, with PFKFB3 identified as a key E2F1-regulated gene crucial for mTORC1 activation.
  • PFKFB3 and PFK1 associate with lysosomes, and PFKFB3 activity modulates mTORC1 lysosomal translocation via interaction with Rag B.

Conclusions:

  • Glucose metabolism, regulated by E2F1 and involving enzymes like PFKFB3, directly impacts mTORC1 activation through lysosomal localization.
  • A glycolytic metabolon at the lysosome acts as a sensor for glucose catabolism, influencing mTORC1 activity.
  • These findings reveal a novel mechanism linking glucose metabolism to cancer cell growth signaling.