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Research article summary (published 21 Oct 2009):

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

Full 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.

 

Author information

Author/s: Fei, Weihua (W); Wang, Han (H); Fu, Xin (X); Bielby, Christopher (C); Yang, Hongyuan (H);

Affiliation: School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney NSW 2052, Australia.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: The Biochemical journal (Biochem J), published in England. (Language: eng)

Reference: 2009-Nov; vol 424 (issue 1) : pp 61-7

Dates: Created 2009/10/20; Completed 2009/11/03;

PMID: 19708857, status: MEDLINE (last retrieval date: 11/3/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Associated Chemicals: Anti-Bacterial Agents (0) ; Membrane Glycoproteins (0) ; Saccharomyces cerevisiae Proteins (0) ; Tunicamycin (11089-65-9) ; Brefeldin A (20350-15-6) ; ARE1 protein, S cerevisiae (EC 2.3.1.26) ; Sterol O-Acyltransferase (EC 2.3.1.26) ; IRE1 protein, S cerevisiae (EC 2.7.10.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)

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