Faculty Opinions recommendation of Fsp27 promotes lipid droplet growth by lipid exchange and transfer at lipid droplet contact sites.

Author(s):  
Thierry Soldati ◽  
Caroline Barisch
2011 ◽  
Vol 195 (6) ◽  
pp. 953-963 ◽  
Author(s):  
Jingyi Gong ◽  
Zhiqi Sun ◽  
Lizhen Wu ◽  
Wenyi Xu ◽  
Nicole Schieber ◽  
...  

Lipid droplets (LDs) are dynamic cellular organelles that control many biological processes. However, molecular components determining LD growth are poorly understood. Genetic analysis has indicated that Fsp27, an LD-associated protein, is important in controlling LD size and lipid storage in adipocytes. In this paper, we demonstrate that Fsp27 is focally enriched at the LD–LD contacting site (LDCS). Photobleaching revealed the occurrence of lipid exchange between contacted LDs in wild-type adipocytes and Fsp27-overexpressing cells but not Fsp27-deficient adipocytes. Furthermore, live-cell imaging revealed a unique Fsp27-mediated LD growth process involving a directional net lipid transfer from the smaller to larger LDs at LDCSs, which is in accordance with the biophysical analysis of the internal pressure difference between the contacting LD pair. Thus, we have uncovered a novel molecular mechanism of LD growth mediated by Fsp27.


Author(s):  
Maya Schuldiner ◽  
Maria Bohnert
Keyword(s):  

2013 ◽  
Vol 24 (4) ◽  
pp. 335-336 ◽  
Author(s):  
William A. Prinz
Keyword(s):  

2015 ◽  
Vol 17 (1) ◽  
pp. 3-3
Author(s):  
Paulina Strzyz

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Ryan S D'Souza ◽  
Jun Y Lim ◽  
Alper Turgut ◽  
Kelly Servage ◽  
Junmei Zhang ◽  
...  

Coordinated assembly and disassembly of integrin-mediated focal adhesions (FAs) is essential for cell migration. Many studies have shown that FA disassembly requires Ca2+ influx, however our understanding of this process remains incomplete. Here, we show that Ca2+ influx via STIM1/Orai1 calcium channels, which cluster near FAs, leads to activation of the GTPase Arf5 via the Ca2+-activated GEF IQSec1, and that both IQSec1 and Arf5 activation are essential for adhesion disassembly. We further show that IQSec1 forms a complex with the lipid transfer protein ORP3, and that Ca2+ influx triggers PKC-dependent translocation of this complex to ER/plasma membrane (PM) contact sites adjacent to FAs. In addition to allosterically activating IQSec1, ORP3 also extracts PI4P from the PM, in exchange for phosphatidylcholine. ORP3-mediated lipid exchange is also important for FA turnover. Together, these findings identify a new pathway that links calcium influx to FA turnover during cell migration.


2019 ◽  
Vol 219 (1) ◽  
Author(s):  
Mike F. Renne ◽  
Brooke M. Emerling

How the distinct lipid composition of organelles is determined and maintained is still poorly understood. In this issue, Du et al. (2019. J. Cell Biol.https://doi.org/10.1083/jcb.201905162) show that the lipid transfer protein ORP5 functions at ER–LD contact sites, regulating lipid droplet levels of phosphatidylserine and phosphatidylinositol-4-phosphate.


BioFactors ◽  
2020 ◽  
Vol 46 (6) ◽  
pp. 943-954
Author(s):  
Wei Xiang ◽  
Shi Cheng ◽  
Yong Zhou ◽  
Ling Ma
Keyword(s):  

2019 ◽  
Vol 132 (12) ◽  
pp. jcs230169 ◽  
Author(s):  
Abdou Rachid Thiam ◽  
Isabelle Dugail

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