2015
DOI: 10.1016/j.jbiotec.2014.08.020
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The characteristics and potential applications of structural lipid droplet proteins in plants

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Cited by 38 publications
(46 citation statements)
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“…(Aubert et al, 2010). Caleosin families were thus named because they possess calcium-binding sites comprised of a helix-loop-helix EF-hand motif (Laibach et al, 2015). Because calcium is a critical factor in the stresssignaling pathway, LD-associated caleosins participate in plant stress responses in addition to their structural role in LDs.…”
Section: Discussionmentioning
confidence: 99%
“…(Aubert et al, 2010). Caleosin families were thus named because they possess calcium-binding sites comprised of a helix-loop-helix EF-hand motif (Laibach et al, 2015). Because calcium is a critical factor in the stresssignaling pathway, LD-associated caleosins participate in plant stress responses in addition to their structural role in LDs.…”
Section: Discussionmentioning
confidence: 99%
“…Numerous plants, insects and microbes synthesize substantial quantities of hydrocarbons such as alkanes, alkenes, and isoprenoids [42-45]. These neutral lipids are likely to partition into the droplet core, although this has only been shown thus far in a few cases [42, 46].…”
Section: 11 What's Inside a Lipid Droplet?mentioning
confidence: 99%
“…These neutral lipids are likely to partition into the droplet core, although this has only been shown thus far in a few cases [42, 46]. For the hydrocarbon precursor of cholesterol, squalene, it has been shown in yeast that its sequestration in LDs is essential for preventing toxicity [47].…”
Section: 11 What's Inside a Lipid Droplet?mentioning
confidence: 99%
“…In plants, the best characterized LD-associated protein is oleosin, which is the most abundant protein on LDs in oilseeds, where LDs accumulate during seed development and then are mobilized following germination in order to provide carbon and energy for seedling growth (Huang, 1996;Siloto et al, 2006;Miquel et al, 2014;Deruyffelaere et al, 2015;Laibach et al, 2015). Oleosins are small, hydrophobic proteins that initially insert cotranslationally into the ER membrane (Beaudoin and Napier, 2002), where, analogous to perilipins, they are thought to help promote the formation of nascent LDs via budding from the ER's outer leaflet, possibly by partitioning neutral lipids within the ER bilayer (Jacquier et al, 2013) and/or aiding in stabilizing the curvature of the ER membrane (Roux et al, 2005).…”
mentioning
confidence: 99%