A sterol-binding protein integrates endosomal lipid metabolism with TOR signaling and nitrogen sensing

Cell. 2012 Feb 17;148(4):702-15. doi: 10.1016/j.cell.2011.12.026.

Abstract

Kes1, and other oxysterol-binding protein superfamily members, are involved in membrane and lipid trafficking through trans-Golgi network (TGN) and endosomal systems. We demonstrate that Kes1 represents a sterol-regulated antagonist of TGN/endosomal phosphatidylinositol-4-phosphate signaling. This regulation modulates TOR activation by amino acids and dampens gene expression driven by Gcn4, the primary transcriptional activator of the general amino acid control regulon. Kes1-mediated repression of Gcn4 transcription factor activity is characterized by nonproductive Gcn4 binding to its target sequences, involves TGN/endosome-derived sphingolipid signaling, and requires activity of the cyclin-dependent kinase 8 (CDK8) module of the enigmatic "large Mediator" complex. These data describe a pathway by which Kes1 integrates lipid metabolism with TORC1 signaling and nitrogen sensing.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autophagy
  • Basic-Leucine Zipper Transcription Factors / metabolism
  • Endosomes / metabolism*
  • Gene Expression Regulation, Fungal
  • Lipid Metabolism*
  • Nitrogen / metabolism*
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Signal Transduction*
  • Sterols / metabolism
  • Transcription Factors / metabolism

Substances

  • Basic-Leucine Zipper Transcription Factors
  • GCN4 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sterols
  • TORC1 protein complex, S cerevisiae
  • Transcription Factors
  • Nitrogen