Conditions of endoplasmic reticulum stress stimulate lipid droplet formation in Saccharomyces cerevisiae.
@article{Fei2009ConditionsOE,
title={Conditions of endoplasmic reticulum stress stimulate lipid droplet formation in Saccharomyces cerevisiae.},
author={Weihua Fei and Han Wang and Xin Fu and Christopher Bielby and Hongyuan Yang},
journal={The Biochemical journal},
year={2009},
volume={424 1},
pages={
61-7
}
}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…
145 Citations
Yeast FIT2 homolog is necessary to maintain cellular proteostasis by regulating lipid homeostasis
- Biology
- 2020
It is suggested that S. cerevisiae FIT homologues may modulate proteostasis and stress response pathways with lipid metabolism at the interface between the two cellular processes.
The yeast FIT2 homologs are necessary to maintain cellular proteostasis and membrane lipid homeostasis
- BiologyJournal of Cell Science
- 2020
A model system to study the role of the Saccharomyces cerevisiae FIT homologues, SCS3 and YFT2, in the proteostasis and stress response pathways is established and data support a model where ScFITs play an important role in lipid metabolism and protestasis beyond their defined roles in LD biogenesis.
c-Flip KO fibroblasts display lipid accumulation associated with endoplasmic reticulum stress.
- BiologyBiochimica et biophysica acta
- 2015
Is fat so bad? Modulation of endoplasmic reticulum stress by lipid droplet formation
- BiologyBiology of the cell
- 2011
The present review focuses on the connections between the basic mechanisms of LD formation and the signal cascades leading to ER stress, and tries to draw possible mechanisms for the role of LDs in the regulation of ER homoeostasis and in ER‐stress‐related diseases.
Endoplasmic reticulum stress and calcium imbalance are involved in cadmium-induced lipid aberrancy in Saccharomyces cerevisiae
- BiologyCell Stress and Chaperones
- 2016
It is concluded that Cd interrupted calcium homeostasis-induced lipid dysregulation leading to ER stress and was confirmed by the increased Kar2p expression.
Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins
- BiologyScientific Reports
- 2019
This work reports that Saccharomyces cerevisiae adapts to lipid bilayer stress by upregulating several protein quality control pathways such as the endoplasmic reticulum-associated degradation (ERAD) pathway and the unfolded protein response (UPR).
Role for Lipid Droplet Biogenesis and Microlipophagy in Adaptation to Lipid Imbalance in Yeast.
- BiologyDevelopmental cell
- 2015
Keeping FIT, storing fat: Lipid droplet biogenesis
- BiologyWorm
- 2016
The recent finding that a conserved family of proteins called fat storage-inducing transmembrane (FIT) proteins is necessary for LDs budding from the ER is discussed, which is critical for understanding the pathophysiology of lipid metabolic disorders like obesity and atherosclerosis.
Endoplasmic reticulum stress induces hepatic steatosis by transcriptional upregulating lipid droplet protein perilipin2
- BiologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
- 2021
It is demonstrated that ER stress could promote LDs accumulation and inhibit lipoprotein transport by transcriptionally upregulating PLIN2 in liver and played an important role in ER stress‐induced hepatic steatosis.
Friend or Foe: Lipid Droplets as Organelles for Protein and Lipid Storage in Cellular Stress Response, Aging and Disease
- BiologyMolecules
- 2020
This work summarizes the current understanding of LDs and their interactions with organelles, providing a storage site for harmful proteins and lipids during cellular stress, aging inflammation and various disease states.
References
SHOWING 1-10 OF 38 REFERENCES
The Lipid-Droplet Proteome Reveals that Droplets Are a Protein-Storage Depot
- BiologyCurrent Biology
- 2006
Caspase-dependent and -independent lipotoxic cell-death pathways in fission yeast
- BiologyJournal of Cell Science
- 2008
This study characterize the sequential molecular events that take place at the onset of cell death in S. pombe, and shows that, under different conditions and stimuli, failure to maintain intracellular-lipid homeostasis can lead to cell death with different phenotypic manifestations, genetic criteria and cellular mechanisms, pointing to the existence of multiple lipotoxic pathways in this organism.
Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum-derived membrane
- BiologyJournal of Cell Science
- 2005
It is suggested that Rab18 regulates LAM formation, which is likely to be involved in mobilizing lipid esters stored in LDs, and the ER membrane apposed to LDs should be named the LD-associated membrane, or LAM.
The unfolded protein response
- BiologyNeurology
- 2006
The ER has evolved highly specific signaling pathways called the unfolded protein response (UPR) to cope with the accumulation of unfolded or mis folded proteins.
Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast
- BiologyThe Journal of cell biology
- 2008
Results suggest that an evolutionally conserved function of seipin in phospholipid metabolism and LD formation may be functionally important in human adipogenesis.
Dynamics of neutral lipid storage in yeast.
- Biology, ChemistryActa biochimica Polonica
- 2004
Besides biochemical properties of enzymes involved in yeast neutral lipid synthesis and degradation, regulatory aspects of these pathways and cell biological consequences of neutral lipid depletion will be discussed in this minireview.
Adipophilin-enriched domains in the ER membrane are sites of lipid droplet biogenesis
- Biology, Environmental ScienceJournal of Cell Science
- 2006
The three-dimensional perspectives provided by freeze-fracture electron microscopy demonstrate unequivocally that at sites of close association, the lipid droplet is not situated within the ER membrane; rather, both ER membranes lie external to and follow the contour of the lipid Droplet, enclosing it in a manner akin to an egg cup holding an egg.
Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals.
- BiologyCurrent opinion in cell biology
- 2001
Functional and Genomic Analyses Reveal an Essential Coordination between the Unfolded Protein Response and ER-Associated Degradation
- BiologyCell
- 2000
Schizosaccharomyces pombe Cells Deficient in Triacylglycerols Synthesis Undergo Apoptosis upon Entry into the Stationary Phase*
- BiologyJournal of Biological Chemistry
- 2003
This study found that two gene products (Plh1p and Dga1p) are responsible for the terminal step of TAG synthesis in the fission yeast Schizosaccharomyces pombe through two different mechanisms, and provides strong evidence suggesting that DAG, not sphingolipids, mediates fatty acids-induced lipoapoptosis in yeast.






