The lipid droplet: A conserved cellular organelle

Zhang, Congyan; Liu, Pingsheng

doi:10.1007/s13238-017-0467-6

Cited by 71 publications

(56 citation statements)

References 54 publications

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“…Lipid droplets (LDs) are a dynamic organelle that widely exists in bacteria, yeast, plants, C. elegans, insects, and mammalian cells [1,2]. It consists of neutral lipid core and phospholipid monolayer membrane which is coated by various types of proteins [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

Rab18 Binds PLIN2 and ACSL3 to Mediate Lipid Droplet Dynamics

Deng

Zhou

Mirza

et al. 2020

Preprint

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Rab18 has been linked to lipid metabolism and metabolic diseases in different model systems, but the mechanism of Rab18-mediated lipid droplet (LD) dynamics in muscle cells remains elusive. Here, we report that Rab18 plays an essential role in oleic acid (OA)-induced LD growth and formation in mouse myoblast cell line C2C12. Rab18 was translocated from endoplasmic reticulum (ER) to LDs during the LD growth induced by OA in C2C12 cells, which was directly regulated by perilipin 2 (PLIN2), a LD resident protein. LD-associated Rab18 bound with the C terminus of PLIN2, and the LD localization of Rab18 was diminished after PLIN2 deletion. Moreover, loss of function of Rab18 led to less triacylglycerol (TAG) accumulation and fewer but larger LD formation. In contrast, expression of wild type Rab18 and a constitutively active Rab18 (Q67L) mutant resulted in elevated TAG content and LD number. Furthermore, LD-associated Rab18 interacted with acyl-CoA synthetase long-chain family member 3 (ACSL3) and in turn, promoted the LD localization of ACSL3, which may play an important role in the accumulation of TAG induced by OA. These data showed that Rab18 was recruited to LD after OA treatment, and formed a complex with PLIN2 and ACSL3, which contributes to TAG accumulating and LD growth.

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Section: Introductionmentioning

confidence: 99%

Rab18 Binds PLIN2 and ACSL3 to Mediate Lipid Droplet Dynamics

Deng

Zhou

Mirza

et al. 2020

Preprint

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“…But the facts that except cytoplasm LDs, the organelle has also been found in several bacteria [18][19][20] that do not have any ER or ER like structures, and more interestingly inside of other cellular organelles such as endoplasmic reticulum (ER), nucleus, chloroplast, and mitochondrion [21][22][23][24][25][26][27], suggesting another possibility that the LD is inheritable, and the origin of the organelle is from prokaryotic cells [28].…”

Section: Introductionmentioning

confidence: 99%

Lipid Droplet Is an Ancient and Inheritable Organelle in Bacteria

Chi

Ogunsade

Zhou

et al. 2020

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Lipid droplet (LD) is a monolayer phospholipid membrane-bound organelle found in all eukaryotes and several prokaryotes which plays key roles in cellular lipid homeostasis and human health. The origin and evolution of the organelle remains unknown. Here, we report that through screening over 660 bacteria using biophysical and biochemical methods, plus LD isolation and proteomic tool, LDs were identified in most of these microbes, affiliated with five main bacterial phyla. Moreover, LDs were also identified in E. coli overexpressing lipid synthesis enzymes, indicating that bacteria without detectable LDs possessed the ability of LD biogenesis. The similarity of isolated LDs from representative strains and evolutionary analysis of LD major protein PspA demonstrate that LDs were conserved in bacteria. Furthermore, time-lapse imaging revealed that LDs were inheritable accompanying with bacterial growth and division. Finally, a common ancestor of LD-containing bacteria was predicted to originate 3.19 billion years ago by a phylogenetic analysis. Our findings suggest that LD is a widespread and inheritable organelle from an ancient common ancestor.

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“…The lipid droplet (LD) is a unique organelle conserved in most organisms from bacteria to humans (Martin and Parton, 2006;Zhang and Liu, 2017). The LD consists of a neutral lipid core of mostly triacylglycerol (TAG), sterol esters, retinyl ester, and/or polyhydroxyalkanoate, surrounded by a monolayer phospholipid membrane and associated proteins (Farese and Walther, 2009).…”

Section: Introductionmentioning

confidence: 99%

Adiposome Targeting and Enzymatic Activity of Lipid Droplet-Specific Proteins

Zhang

et al. 2020

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RUNNING TITLESProtein targeting to adiposomes and enzymatic activity. ABBREVIATIONS DOPC: 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine. DOPE: 1,2-di-(9Z-octadecenoyl)-sn-glycero-3phosphoethanolamine. PI: phosphatidylinositol. Liver PI: L-α-phosphatidylinositol (Liver, Bovine) (sodium salt). TAG: triacylglycerol. ADRP: adipose differentiation-related protein. TIP47: tail-interacting protein of 47 kDa. PLINs: perilipin family proteins. ATGL: adipose triglyceride lipase. ALD: artificial lipid droplet. LD: lipid droplet. FFF-MALS: 2 field flow fractionation-multi-angle light scattering. TEM: Transmission electron microscope. SUMMARYNew strategies to decode the specific protein targeting mechanism on lipid droplet (LD) are urgently needed.Using adiposome, the LD binding of perilipin 2 (PLIN2), perilipin 3 (PLIN3), and adipose triglyceride lipase (ATGL) were studied. Scatchard analysis found that the binding of PLIN2 to the adiposome surface was saturable, pointing to a specific membrane binding partner. Phosphatidylinositol (PI) was found to inhibit PLIN2 binding while it did not impede PLIN3. Structural analysis combined with mutagenesis revealed that the 73 rd glutamic acid of PLIN2 is significant for the effect of PI on the protein binding. The presence of PI significantly stimulated the activity of ATGL in vitro. The phosphorylation site mutants of ATGL were found reducing the lipase activity in the adiposome system. Our study demonstrates the utility of adiposome as a powerful, manipulatable model system for the characterization of LD binding and enzymatic activity of LD proteins in vitro.

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The lipid droplet: A conserved cellular organelle

Cited by 71 publications

References 54 publications

Rab18 Binds PLIN2 and ACSL3 to Mediate Lipid Droplet Dynamics

Rab18 Binds PLIN2 and ACSL3 to Mediate Lipid Droplet Dynamics

Lipid Droplet Is an Ancient and Inheritable Organelle in Bacteria

Adiposome Targeting and Enzymatic Activity of Lipid Droplet-Specific Proteins

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