Lipid droplet metabolism

Khor, Victor K.; Shen, Wen-Jun; Kraemer, Fredric B.

doi:10.1097/mco.0b013e3283651106

Cited by 90 publications

(62 citation statements)

References 46 publications

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“…LDs are unique subcellular organelles that compartmentalize a variety of hydrophobic compounds in plants, including TAGs, steryl esters, and polyisoprenoids (Murphy, 2012;Khor et al, 2013). While the majority of our knowledge regarding the biogenesis and function of these organelles in plants comes from studies of oilseeds, there is increasing appreciation that LDs also play important and dynamic roles in a variety of other physiological processes within the vegetative tissues and organs of plants (Shimada et al, 2014.…”

Section: Discussionmentioning

confidence: 99%

Lipid Droplet-Associated Proteins (LDAPs) Are Required for the Dynamic Regulation of Neutral Lipid Compartmentation in Plant Cells

et al. 2016

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Eukaryotic cells compartmentalize neutral lipids into organelles called lipid droplets (LDs), and while much is known about the role of LDs in storing triacylglycerols in seeds, their biogenesis and function in nonseed tissues are poorly understood. Recently, we identified a class of plant-specific, lipid droplet-associated proteins (LDAPs) that are abundant components of LDs in nonseed cell types. Here, we characterized the three LDAPs in Arabidopsis (Arabidopsis thaliana) to gain insight to their targeting, assembly, and influence on LD function and dynamics. While all three LDAPs targeted specifically to the LD surface, truncation analysis of LDAP3 revealed that essentially the entire protein was required for LD localization. The association of LDAP3 with LDs was detergent sensitive, but the protein bound with similar affinity to synthetic liposomes of various phospholipid compositions, suggesting that other factors contributed to targeting specificity. Investigation of LD dynamics in leaves revealed that LD abundance was modulated during the diurnal cycle, and characterization of LDAP misexpression mutants indicated that all three LDAPs were important for this process. LD abundance was increased significantly during abiotic stress, and characterization of mutant lines revealed that LDAP1 and LDAP3 were required for the proper induction of LDs during heat and cold temperature stress, respectively. Furthermore, LDAP1 was required for proper neutral lipid compartmentalization and triacylglycerol degradation during postgerminative growth. Taken together, these studies reveal that LDAPs are required for the maintenance and regulation of LDs in plant cells and perform nonredundant functions in various physiological contexts, including stress response and postgerminative growth.

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Section: Discussionmentioning

confidence: 99%

Lipid Droplet-Associated Proteins (LDAPs) Are Required for the Dynamic Regulation of Neutral Lipid Compartmentation in Plant Cells

et al. 2016

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“…45 Lipolysis requires the recruitment of lipases and their activators to the lipid droplet, and interactions with lipid droplet-associated proteins for access to the triglyceride substrate (Fig. 2).…”

Section: Cellular and Molecular Control Of Adipose Tissue Metabolismmentioning

confidence: 99%

Exercise and the Regulation of Adipose Tissue Metabolism

Tsiloulis

Watt

2015

Progress in Molecular Biology and Translational Science

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“…IBs formed in cells infected with rotaviruses are based on lipid droplets (32,50), subcellular organelles important for lipid storage and metabolism. Our previous study indicated that the IBs formed in SFTSV infection are built on the foundation of lipid droplets as well (23).…”

Section: Discussionmentioning

confidence: 99%

Synaptogyrin-2 Promotes Replication of a Novel Tick-borne Bunyavirus through Interacting with Viral Nonstructural Protein NSs

Sun

Zhang

et al. 2016

Journal of Biological Chemistry

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Synaptogyrin-2 is a non-neuronal member of the synaptogyrin family involved in synaptic vesicle biogenesis and trafficking. Little is known about the function of synaptogyrin-2. Severe fever with thrombocytopenia syndrome (SFTS) is an emerging infectious disease characterized by high fever, thrombocytopenia, and leukocytopenia with high mortality, caused by a novel tick-borne phlebovirus in the family Bunyaviridae. Our previous studies have shown that the viral nonstructural protein NSs forms inclusion bodies (IBs) that are involved in viral immune evasion, as well as viral RNA replication. In this study, we sought to elucidate the mechanism by which NSs formed the IBs, a lipid droplet-based structure confirmed by NSs co-localization with perilipin A and adipose differentiation-related protein (ADRP). Through a high throughput screening, we identified synaptogyrin-2 to be highly up-regulated in response to SFTS bunyavirus (SFTSV) infection and to be a promoter of viral replication. We demonstrated that synaptogyrin-2 interacted with NSs and was translocated into the IBs, which were reconstructed from lipid droplets into large structures in infection. Viral RNA replication decreased, and infectious virus titers were lowered significantly when synaptogyrin-2 was silenced in specific shRNAexpressing cells, which correlated with the reduced number of the large IBs restructured from regular lipid droplets. We hypothesize that synaptogyrin-2 is essential to promoting the formation of the IBs to become virus factories for viral RNA replication through its interaction with NSs. These findings unveil the function of synaptogyrin-2 as an enhancer in viral infection. Synaptogyrin-2 (SYNGR2)2 is a tetraspan vesicle membrane protein (1-3) and a member of the synaptogyrin family. Synaptogyrin-1 and -3, abundantly present in synaptic vesicles, are believed to be involved in various aspects in the synaptic vesicle cycle, including vesicle biogenesis, exocytosis and endocytotic recycling, and neurotransmission (2, 4). They are encoded by multigene classes in mammals and evolutionarily conserved throughout the animal kingdom (5). The synaptogyrin-2 gene transcript of 1.6 kb is expressed at high levels in all tissues, except brain, encoding a protein of 224 amino acids in length (5). However, studies on synaptogyrin-2 have been limited, and the function of this protein is largely unknown.Emerging tick-borne bunyaviruses have been recognized to be a serious threat to public health and include severe fever with thrombocytopenia syndrome virus (SFTSV) (6). Since first identified in 2010 in China (7), SFTSV has caused over 3000 reported cases with mortalities ranging from 5 to 15% and has quickly spread to more than 13 provinces (8, 9). Although the symptoms of SFTS are mainly nonspecific, drastic loss of white blood cells and platelets are reported in most cases, and multiorgan failure can occur in severe cases, which usually are fatal (10, 11). SFTSV has also been isolated from patients in Korea and Japan since 2013 (12-15). The clo...

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Lipid droplet metabolism

Cited by 90 publications

References 46 publications

Lipid Droplet-Associated Proteins (LDAPs) Are Required for the Dynamic Regulation of Neutral Lipid Compartmentation in Plant Cells

Lipid Droplet-Associated Proteins (LDAPs) Are Required for the Dynamic Regulation of Neutral Lipid Compartmentation in Plant Cells

Exercise and the Regulation of Adipose Tissue Metabolism

Synaptogyrin-2 Promotes Replication of a Novel Tick-borne Bunyavirus through Interacting with Viral Nonstructural Protein NSs

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