Lin28 enhances de novo fatty acid synthesis to promote cancer progression via SREBP-1

EMBO Rep. 2019 Oct 4;20(10):e48115. doi: 10.15252/embr.201948115. Epub 2019 Aug 5.

Abstract

Lin28 plays an important role in promoting tumor development, whereas its exact functions and underlying mechanisms are largely unknown. Here, we show that both human homologs of Lin28 accelerate de novo fatty acid synthesis and promote the conversion from saturated to unsaturated fatty acids via the regulation of SREBP-1. By directly binding to the mRNAs of both SREBP-1 and SCAP, Lin28A/B enhance the translation and maturation of SREBP-1, and protect cancer cells from lipotoxicity. Lin28A/B-stimulated tumor growth is abrogated by SREBP-1 inhibition and by the impairment of the RNA binding properties of Lin28A/B, respectively. Collectively, our findings uncover that post-transcriptional regulation by Lin28A/B enhances de novo fatty acid synthesis and metabolic conversion of saturated and unsaturated fatty acids via SREBP-1, which is critical for cancer progression.

Keywords: Lin28; SREBP cleavage-activating protein; SREBP-1; de novo fatty acid synthesis; lipotoxicity; saturated and unsaturated fatty acids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line, Tumor
  • Cell Proliferation
  • Cytoprotection
  • Disease Progression*
  • Endoplasmic Reticulum Stress
  • Fatty Acids / biosynthesis*
  • Humans
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Liver Neoplasms / metabolism*
  • Liver Neoplasms / pathology*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Models, Biological
  • Protein Binding
  • Protein Biosynthesis
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA-Binding Proteins / metabolism*
  • Sterol Regulatory Element Binding Protein 1 / metabolism*

Substances

  • Fatty Acids
  • Intracellular Signaling Peptides and Proteins
  • Lin28A protein, human
  • Membrane Proteins
  • RNA, Messenger
  • RNA-Binding Proteins
  • SREBP cleavage-activating protein
  • Sterol Regulatory Element Binding Protein 1