Acyl-CoA synthetase 3 promotes lipid droplet biogenesis in ER microdomains

Kassan, Adam, Herms, Albert, Fernandez-Vidal, Andrea, Bosch, Marta, Schieber, Nicole L., Reddy, Babu J. N., Fajardo, Alba, Gelabert-Baldrich, Mariona, Tebar, Francesc, Enrich, Carlos, Gross, Steven P., Parton, Robert G. and Pol, Albert (2013) Acyl-CoA synthetase 3 promotes lipid droplet biogenesis in ER microdomains. Journal of Cell Biology, 203 6: 985-1001. doi:10.1083/jcb.201305142

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Author Kassan, Adam
Herms, Albert
Fernandez-Vidal, Andrea
Bosch, Marta
Schieber, Nicole L.
Reddy, Babu J. N.
Fajardo, Alba
Gelabert-Baldrich, Mariona
Tebar, Francesc
Enrich, Carlos
Gross, Steven P.
Parton, Robert G.
Pol, Albert
Title Acyl-CoA synthetase 3 promotes lipid droplet biogenesis in ER microdomains
Journal name Journal of Cell Biology   Check publisher's open access policy
ISSN 0021-9525
Publication date 2013-12-23
Year available 2013
Sub-type Article (original research)
DOI 10.1083/jcb.201305142
Open Access Status File (Publisher version)
Volume 203
Issue 6
Start page 985
End page 1001
Total pages 17
Place of publication New York, NY, United States
Publisher Rockefeller University Press
Language eng
Subject 1307 Cell Biology
Abstract Control of lipid droplet (LD) nucleation and copy number are critical, yet poorly understood, processes. We use model peptides that shift from the endoplasmic reticulum (ER) to LDs in response to fatty acids to characterize the initial steps of LD formation occurring in lipid-starved cells. Initially, arriving lipids are rapidly packed in LDs that are resistant to starvation (pre-LDs). Pre-LDs are restricted ER microdomains with a stable core of neutral lipids. Subsequently, a first round of “emerging” LDs is nucleated, providing additional lipid storage capacity. Finally, in proportion to lipid concentration, new rounds of LDs progressively assemble. Confocal microscopy and electron tomography suggest that emerging LDs are nucleated in a limited number of ER microdomains after a synchronized stepwise process of protein gathering, lipid packaging, and recognition by Plin3 and Plin2. A comparative analysis demonstrates that the acyl-CoA synthetase 3 is recruited early to the assembly sites, where it is required for efficient LD nucleation and lipid storage
Keyword Cell Biology
Cell Biology
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID BFU2011-23745
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
Institute for Molecular Bioscience - Publications
Centre for Microscopy and Microanalysis Publications
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Citation counts: TR Web of Science Citation Count  Cited 66 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 24 Jan 2014, 01:29:39 EST by Susan Allen on behalf of Institute for Molecular Bioscience