scholarly journals Multifunctional pyrazoline based AIEgens: real-time tracking and specific protein “fishing” of lipid droplets

2019 ◽  
Vol 10 (39) ◽  
pp. 9009-9016 ◽  
Author(s):  
Na Zhao ◽  
Yan Li ◽  
Weiyao Yang ◽  
Jiabao Zhuang ◽  
Yue Li ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Real Time ◽  
Intracellular Ph ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
Specific Protein ◽  
Related Protein ◽  
Dual Color ◽  
Real Time Tracking

A series of multifunctional pyrazoline based AIEgens were developed for real-time tracking of lipid metabolism, reversibly monitoring intracellular pH in dual-color mode and specific labeling of lipid droplet related protein.

Real-time tracking of lipid droplets interactions with other organelles by a high signal/noise probe

2021 ◽  
pp. 109366
Author(s):  
Wei Ren ◽  
Dong Wang ◽  
Wei Huang ◽  
Jiajia Li ◽  
Xiaohe Tian ◽  
...  
Keyword(s):  
Real Time ◽  
Lipid Droplets ◽  
High Signal ◽  
Signal Noise ◽  
Real Time Tracking

scholarly journals A conserved family of proteins facilitates nascent lipid droplet budding from the ER

2015 ◽  
Vol 211 (2) ◽  
pp. 261-271 ◽  
Author(s):  
Vineet Choudhary ◽  
Namrata Ojha ◽  
Andy Golden ◽  
William A. Prinz
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Lipid Metabolism ◽  
Caenorhabditis Elegans ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
De Novo ◽  
Fat Storage ◽  
Higher Eukaryotes ◽  
Er Membrane

Lipid droplets (LDs) are found in all cells and play critical roles in lipid metabolism. De novo LD biogenesis occurs in the endoplasmic reticulum (ER) but is not well understood. We imaged early stages of LD biogenesis using electron microscopy and found that nascent LDs form lens-like structures that are in the ER membrane, raising the question of how these nascent LDs bud from the ER as they grow. We found that a conserved family of proteins, fat storage-inducing transmembrane (FIT) proteins, is required for proper budding of LDs from the ER. Elimination or reduction of FIT proteins in yeast and higher eukaryotes causes LDs to remain in the ER membrane. Deletion of the single FIT protein in Caenorhabditis elegans is lethal, suggesting that LD budding is an essential process in this organism. Our findings indicated that FIT proteins are necessary to promote budding of nascent LDs from the ER.

Mouse Fat-Specific Protein 27 (FSP27) expressed in plant cells localizes to lipid droplets and promotes lipid droplet accumulation and fusion

Biochimie ◽  
2020 ◽  
Vol 169 ◽  
pp. 41-53 ◽  
Author(s):  
Ann M. Price ◽  
Nathan M. Doner ◽  
Satinder K. Gidda ◽  
Srikarthika Jambunathan ◽  
Christopher N. James ◽  
...  
Keyword(s):  
Lipid Droplet ◽  
Lipid Droplets ◽  
Plant Cells ◽  
Specific Protein

scholarly journals Perilipin-related protein regulates lipid metabolism in C. elegans

2015 ◽  
Author(s):  
Ahmed A. Chughtai ◽  
Filip Kaššák ◽  
Markéta Kostrouchová ◽  
Jan Philipp Novotný ◽  
Michael W. Krause ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Lipid Droplets ◽  
Fat Metabolism ◽  
Droplet Surface ◽  
Surface Proteins ◽  
Related Protein ◽  
Additional Mechanism ◽  
C Elegans ◽  
Functional Studies ◽  
Gene Inhibition

The perilipins are lipid droplet surface proteins that contribute to fat metabolism by controlling the access of lipids to lipolytic enzymes. Perilipins have been identified in organisms as diverse as metazoa, fungi, and amoebas but strikingly not in nematodes. Here we identify the protein encoded by the W01A8.1 gene in Caenorhabditis elegans as the closest homologue of metazoan perilipin. We demonstrate that nematode W01A8.1 is a cytoplasmic protein residing on lipid droplets. Human perilipins 1 and 2 localize in transgenic C. elegans on the same structures as proteins expressed from W01A8.1 gene. Inhibition and elimination of W01A8.1 affects the appearance of lipid droplets especially visible as the formation of large lipid droplets localized around the dividing nucleus during the early zygotic divisions. This phenomenon disappears in later stages of embryogenesis indicating the existence of an additional mechanism of lipid regulation in C. elegans. Our results demonstrate that perilipin-related regulation of fat metabolism is conserved in nematodes and provide new possibilities for functional studies of lipid metabolism.

scholarly journals Seipin-Mediated Contacts as Gatekeepers of Lipid Flux at the Endoplasmic Reticulum–Lipid Droplet Nexus 

Contact ◽  
2020 ◽  
Vol 3 ◽  
pp. 251525642094582
Author(s):  
Veijo T. Salo ◽  
Maarit Hölttä-Vuori ◽  
Elina Ikonen
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Metabolism ◽  
Recent Work ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
Intimate Relationship

Lipid droplets (LDs) are dynamic cellular hubs of lipid metabolism. While LDs contact a plethora of organelles, they have the most intimate relationship with the endoplasmic reticulum (ER). Indeed, LDs are initially assembled at specialized ER subdomains, and recent work has unraveled an increasing array of proteins regulating ER-LD contacts. Among these, seipin, a highly conserved lipodystrophy protein critical for LD growth and adipogenesis, deserves special attention. Here, we review recent insights into the role of seipin in LD biogenesis and as a regulator of ER-LD contacts. These studies have also highlighted the evolving concept of ER and LDs as a functional continuum for lipid partitioning and pinpointed a role for seipin at the ER-LD nexus in controlling lipid flux between these compartments.

scholarly journals Perilipin-related protein regulates lipid metabolism in C. elegans

2015 ◽  
Author(s):  
Ahmed A. Chughtai ◽  
Filip Kaššák ◽  
Markéta Kostrouchová ◽  
Jan Philipp Novotný ◽  
Michael W. Krause ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Lipid Droplets ◽  
Fat Metabolism ◽  
Droplet Surface ◽  
Surface Proteins ◽  
Related Protein ◽  
Additional Mechanism ◽  
C Elegans ◽  
Functional Studies ◽  
Gene Inhibition

The perilipins are lipid droplet surface proteins that contribute to fat metabolism by controlling the access of lipids to lipolytic enzymes. Perilipins have been identified in organisms as diverse as metazoa, fungi, and amoebas but strikingly not in nematodes. Here we identify the protein encoded by the W01A8.1 gene in Caenorhabditis elegans as the closest homologue of metazoan perilipin. We demonstrate that nematode W01A8.1 is a cytoplasmic protein residing on lipid droplets. Human perilipins 1 and 2 localize in transgenic C. elegans on the same structures as proteins expressed from W01A8.1 gene. Inhibition and elimination of W01A8.1 affects the appearance of lipid droplets especially visible as the formation of large lipid droplets localized around the dividing nucleus during the early zygotic divisions. This phenomenon disappears in later stages of embryogenesis indicating the existence of an additional mechanism of lipid regulation in C. elegans. Our results demonstrate that perilipin-related regulation of fat metabolism is conserved in nematodes and provide new possibilities for functional studies of lipid metabolism.

scholarly journals Getting a handle on lipid droplets: Insights into ER–lipid droplet tethering

2019 ◽  
Vol 218 (4) ◽  
pp. 1089-1091 ◽  
Author(s):  
Truc B. Nguyen ◽  
James A. Olzmann
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Metabolism ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
Human Cells ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Cell Biol ◽  
Membrane Contact

Lipid droplets (LDs) are hubs for lipid metabolism that form membrane contact sites with multiple organelles. In this issue, Hariri et al. (2019. J. Cell Biol. https://doi.org/10.1083/jcb.201808119) reveal the functions of Mdm1-mediated endoplasmic reticulum (ER)–LD tethering in yeast and Datta et al. (2019. J. Cell Biol. https://doi.org/10.1083/jcb.201808133) identify a role for the Mdm1 orthologue, Snx14, as an ER–LD tether that regulates lipid metabolism in human cells.

scholarly journals HCV Pit Stop at the Lipid Droplet: Refuel Lipids and Put on a Lipoprotein Coat before Exit

Cells ◽  
2019 ◽  
Vol 8 (3) ◽  
pp. 233 ◽  
Author(s):  
Gabrielle Vieyres ◽  
Thomas Pietschmann
Keyword(s):  
Lipid Metabolism ◽  
Lipid Droplet ◽  
Cell Biology ◽  
Lipid Droplets ◽  
Protein Translocation ◽  
Droplet Surface ◽  
Replication Cycle ◽  
Virion Assembly ◽  
Host Interactions ◽  
Virus Replication Cycle

The replication cycle of the liver-tropic hepatitis C virus (HCV) is tightly connected to the host lipid metabolism, during the virus entry, replication, assembly and egress stages, but also while the virus circulates in the bloodstream. This interplay coins viral particle properties, governs viral cell tropism, and facilitates immune evasion. This review summarizes our knowledge of these interactions focusing on the late steps of the virus replication cycle. It builds on our understanding of the cell biology of lipid droplets and the biosynthesis of liver lipoproteins and attempts to explain how HCV hijacks these organelles and pathways to assemble its lipo-viro-particles. In particular, this review describes (i) the mechanisms of viral protein translocation to and from the lipid droplet surface and the orchestration of an interface between replication and assembly complexes, (ii) the importance of the triglyceride mobilization from the lipid droplets for HCV assembly, (iii) the interplay between HCV and the lipoprotein synthesis pathway including the role played by apolipoproteins in virion assembly, and finally (iv) the consequences of these complex virus–host interactions on the virion composition and its biophysical properties. The wealth of data accumulated in the past years on the role of the lipid metabolism in HCV assembly and its imprint on the virion properties will guide vaccine design efforts and reinforce our understanding of the hepatic lipid metabolism in health and disease.

scholarly journals Lipid Droplets Define a Sub-Population of Breast Cancer Stem Cells

2019 ◽  
Vol 9 (1) ◽  
pp. 87 ◽  
Author(s):  
Benjamin J. Hershey ◽  
Roberta Vazzana ◽  
Débora L. Joppi ◽  
Kristina M. Havas
Keyword(s):  
Breast Cancer ◽  
Stem Cells ◽  
Stem Cell ◽  
Lipid Metabolism ◽  
Cancer Stem Cells ◽  
Cancer Stem Cell ◽  
Cell Lines ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
Breast Cancer Stem Cells

Tumor recurrence is now the leading cause of breast cancer-related death. These recurrences are believed to arise from residual cancer stem cells that survive initial therapeutic intervention. Therefore, a comprehensive understanding of cancer stem cell biology is needed to generate more effective therapies. Here we investigate the association between dysregulation of lipid metabolism and breast cancer stem cells. Focusing specifically on lipid droplets, we found that the lipid droplet number correlates with stemness in a panel of breast cell lines. Using a flow cytometry-based method developed for this study, we establish a means to isolate cells with augmented lipid droplet loads from total populations and show that they are enriched in cancer stem cells. Furthermore, pharmacological targeting of fatty acid metabolism reveals a metabolic addiction in a subset of cell lines. Our results highlight a key role for the lipid metabolism in the maintenance of the breast cancer stem cell pool, and as such, suggest it as a potential therapeutic target.

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