Utilizad este identificador para citar o enlazar este documento: http://hdl.handle.net/2072/232911

Acyl-CoA synthetase 3 promotes lipid droplet biogenesis in ER microdomains.
Kassan, A.; Herms, A.; Fernández-Vidal, A.; Bosch, M.; Schieber, N.L.; Reddy, B.J.; Fajardo, A.; Gelabert-Baldrich, M.; Tebar Ramon, Francesc; Enrich Bastús, Carles; Gross, S.P.; Parton, R.G.; Pol i Sorolla, Albert
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.
13-06-2014
Coenzims
Metabolisme dels lípids
Transport biològic
Coenzymes
Lipid metabolism
Biological transport
cc-by (c) Kassan, A. et al., 2013
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/embargoedAccess
Artículo
info:eu-repo/semantics/publishedVersion
Rockefeller University Press
         

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Kassan, A.; Herms, A.; Fernández-Vidal, A.; Bosch, M.; Schieber, N.L.; Reddy, B.J.; Fajardo, A.; Gelabert-Baldrich, M.; Tebar Ramon, Francesc; Enrich Bastús, Carles; Gross, S.P.; Parton, R.G.; Pol i Sorolla, Albert
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