Conditions of endoplasmic reticulum stress stimulate lipid droplet formation in Saccharomyces cerevisiae

Biochem J. 2009 Oct 23;424(1):61-7. doi: 10.1042/BJ20090785.

Abstract

LDs (lipid droplets) are cellular organelles which can be found in nearly all eukaryotic cells. Despite their importance in cell biology, the mechanism underlying LD biogenesis remains largely unknown. In the present study we report that conditions of ER (endoplasmic reticulum) stress stimulate LD formation in Saccharomyces cerevisiae. We found that LDs accumulated in yeast mutants with compromised protein glycosylation or ER-associated protein degradation. Moreover, tunicamycin and Brefeldin A, agents which induce ER stress, were found to stimulate LD formation. In contrast, the restoration of protein glycosylation reduced LD accumulation. Interestingly, enhanced neutral lipids synthesis and LD formation under conditions of ER stress was not dependent on Ire1p. Lastly, we demonstrated that the absence of LDs did not compromise cell viability under ER stress. Our results suggest that although more LDs are produced, LDs are not essential to cell survival under ER stress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Blotting, Western
  • Brefeldin A / pharmacology
  • Endoplasmic Reticulum / drug effects
  • Endoplasmic Reticulum / genetics
  • Endoplasmic Reticulum / metabolism*
  • Lipid Metabolism / drug effects
  • Lipid Metabolism / genetics
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / physiology
  • Mutation
  • Organelles / drug effects
  • Organelles / metabolism*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / physiology
  • Reverse Transcriptase Polymerase Chain Reaction
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / physiology
  • Sterol O-Acyltransferase / metabolism
  • Tunicamycin / pharmacology

Substances

  • Anti-Bacterial Agents
  • Membrane Glycoproteins
  • Saccharomyces cerevisiae Proteins
  • Tunicamycin
  • Brefeldin A
  • ARE1 protein, S cerevisiae
  • Sterol O-Acyltransferase
  • IRE1 protein, S cerevisiae
  • Protein Serine-Threonine Kinases