PML isoform II plays a critical role in nuclear lipid droplet formation

Ohsaki, Yuki; Kawai, Takeshi; Yoshikawa, Yukichika; Cheng, Jinglei; Jokitalo, Eija; Fujimoto, Toyoshi

doi:10.1083/jcb.201507122

Cited by 155 publications

(267 citation statements)

References 47 publications

(66 reference statements)

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“…It was difficult to distinguish these possibilities using fluorescence microscopy. Recent studies using electron microscopy of serial sections has revealed that LDs may indeed reside within the nucleoplasm [42,44]. Nuclear LDs may be limited to specific cell types.…”

Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

“…Nuclear LDs may be limited to specific cell types. They have been detected in human liver and human and mouse hepatic cell lines, but are much less abundant in fibroblasts and adipocytes [42,44]. Nuclear LDs appear to localize with protrusions from the inner nuclear cell membrane, and depend on SUN proteins and PML (promyelocytic leukemia) bodies for formation [44].…”

Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

“…They have been detected in human liver and human and mouse hepatic cell lines, but are much less abundant in fibroblasts and adipocytes [42,44]. Nuclear LDs appear to localize with protrusions from the inner nuclear cell membrane, and depend on SUN proteins and PML (promyelocytic leukemia) bodies for formation [44]. It appears that there is capacity for expansion of LDs locally within the nucleus, as nuclear LDs co-localize both with DGAT2 and with the rate-limiting enzyme for phosphatidylcholine synthesis in the CDP-choline pathway, phosphocholine cytidylyltransferase [44].…”

Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

“…Nuclear LDs appear to localize with protrusions from the inner nuclear cell membrane, and depend on SUN proteins and PML (promyelocytic leukemia) bodies for formation [44]. It appears that there is capacity for expansion of LDs locally within the nucleus, as nuclear LDs co-localize both with DGAT2 and with the rate-limiting enzyme for phosphatidylcholine synthesis in the CDP-choline pathway, phosphocholine cytidylyltransferase [44]. Fatty acyl-CoAs are also present in the nucleus [45,46], and AGPAT3, AGPAT5, lipin 1 and lipin 3 can all localize to the nucleus [26,44].…”

Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

“…It appears that there is capacity for expansion of LDs locally within the nucleus, as nuclear LDs co-localize both with DGAT2 and with the rate-limiting enzyme for phosphatidylcholine synthesis in the CDP-choline pathway, phosphocholine cytidylyltransferase [44]. Fatty acyl-CoAs are also present in the nucleus [45,46], and AGPAT3, AGPAT5, lipin 1 and lipin 3 can all localize to the nucleus [26,44]. Lipin 1 has been shown to have a nuclear role outside of lipid synthesis, acting as a transcriptional modulator in conjunction with nuclear receptors and transcriptional coactivators.…”

Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

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How lipid droplets “TAG” along: Glycerolipid synthetic enzymes and lipid storage

Wang

Airola

Reue

2017

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Triacylglycerols (TAG) serve as the predominant form of energy storage in mammalian cells, and TAG synthesis influences conditions such as obesity, fatty liver, and insulin resistance. In most tissues, the glycerol 3-phosphate pathway enzymes are responsible for TAG synthesis, and the regulation and function of these enzymes is therefore important for metabolic homeostasis. Here we review the sites and regulation of glycerol-3-phosphate acyltransferase (GPAT), acylglycerol-3-phosphate acyltransferase (AGPAT), lipin/phosphatidic acid phosphatase (PAP), and diacylglycerol acyltransferase (DGAT) enzyme action. We highlight the critical roles that these enzymes play in human health by reviewing Mendelian disorders that result from mutation in the corresponding genes. We also summarize the valuable insights that genetically engineered mouse models have provided into the cellular and physiological roles of GPATs, AGPATs, lipins and DGATs. Finally, we comment on the status and feasibility of therapeutic approaches to metabolic disease that target enzymes of the glycerol 3-phosphate pathway.

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Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

Section: Overview Of the Glycerol 3-phosphate Pathway For Lipid Symentioning

confidence: 99%

See 3 more Smart Citations

How lipid droplets “TAG” along: Glycerolipid synthetic enzymes and lipid storage

Wang

Airola

Reue

2017

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Molecular mechanisms of perilipin protein function in lipid droplet metabolism

Griseti,

Bello,

Bieth

et al. 2024

FEBS Letters

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Perilipins are abundant lipid droplet (LD) proteins present in all metazoans and also in Amoebozoa and fungi. Humans express five perilipins, which share a similar domain organization: an amino‐terminal PAT domain and an 11‐mer repeat region, which can fold into amphipathic helices that interact with LDs, followed by a structured carboxy‐terminal domain. Variations of this organization that arose during vertebrate evolution allow for functional specialization between perilipins in relation to the metabolic needs of different tissues. We discuss how different features of perilipins influence their interaction with LDs and their cellular targeting. PLIN1 and PLIN5 play a direct role in lipolysis by regulating the recruitment of lipases to LDs and LD interaction with mitochondria. Other perilipins, particularly PLIN2, appear to protect LDs from lipolysis, but the molecular mechanism is not clear. PLIN4 stands out with its long repetitive region, whereas PLIN3 is most widely expressed and is used as a nascent LD marker. Finally, we discuss the genetic variability in perilipins in connection with metabolic disease, prominent for PLIN1 and PLIN4, underlying the importance of understanding the molecular function of perilipins.

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The lipid droplet lipidome

Wölk,

Fedorova

2024

FEBS Letters

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Lipid droplets (LDs) are intracellular organelles with a hydrophobic core formed by neutral lipids surrounded by a phospholipid monolayer harboring a variety of regulatory and enzymatically active proteins. Over the last few decades, our understanding of LD biology has evolved significantly. Nowadays, LDs are appreciated not just as passive energy storage units, but rather as active players in the regulation of lipid metabolism and quality control machineries. To fulfill their functions in controlling cellular metabolic states, LDs need to be highly dynamic and responsive organelles. A large body of evidence supports a dynamic nature of the LD proteome and its contact sites with other organelles. However, much less is known about the lipidome of LDs. Numerous examples clearly indicate the intrinsic link between LD lipids and proteins, calling for a deeper characterization of the LD lipidome in various physiological and pathological settings. Here, we reviewed the current state of knowledge in the field of the LD lipidome, providing a brief overview of the lipid classes and their molecular species present within the neutral core and phospholipid monolayer.

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PML isoform II plays a critical role in nuclear lipid droplet formation

Abstract: PML-II plays a critical role in generating nuclear lipid droplets, which are associated with promyelocytic leukemia nuclear bodies as well as with the extension of the inner nuclear membrane.

Cited by 155 publications

References 47 publications

How lipid droplets “TAG” along: Glycerolipid synthetic enzymes and lipid storage

How lipid droplets “TAG” along: Glycerolipid synthetic enzymes and lipid storage

Molecular mechanisms of perilipin protein function in lipid droplet metabolism

The lipid droplet lipidome

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