scholarly journals Regulation of lipid droplet dynamics in Saccharomyces cerevisiae depends on the Rab7-like Ypt7p, HOPS complex and V1-ATPase

Biology Open ◽  
2015 ◽  
Vol 4 (7) ◽  
pp. 764-775 ◽  
Author(s):  
I. Bouchez ◽  
M. Pouteaux ◽  
M. Canonge ◽  
M. Genet ◽  
T. Chardot ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Lipid Droplet ◽  
Droplet Dynamics ◽  
V1 Atpase ◽  
Hops Complex

Tracking lipid droplet dynamics for the discrimination of cancer cells by a solvatochromic fluorescent probe

2021 ◽  
Vol 333 ◽  
pp. 129541
Author(s):  
Linlin Yang ◽  
Jianping Wang ◽  
Bianhua Liu ◽  
Guangmei Han ◽  
Hong Wang ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Fluorescent Probe ◽  
Lipid Droplet ◽  
Droplet Dynamics

scholarly journals Molecular modelling, docking and dynamics analysis of lipid droplet associated enzyme Ypr147cp from Saccharomyces cerevisiae

2021 ◽  
Vol 17 (1) ◽  
pp. 132-138
Author(s):  
Naresh Kumar Manda ◽  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Lipid Droplet ◽  
Covalent Binding ◽  
Microscopic Analysis ◽  
Homology Model ◽  
Lipid Profiling ◽  
Electron Microscopic ◽  
Triacylglycerol Lipase ◽  
Knock Out ◽  
Transmission Electron Microscopic Analysis

Ypr147cp of Saccharomyces cerevisiae was localized to lipid droplets. The recombinant Ypr147cp showed both triacylglycerol lipase and ester hydrolase activities. Knock out of YPR147C led to accumulation of TAG in ypr147cΔ when compared to wild type (WT). Transmission electron microscopic analysis of ypr147cΔ cells show increased lipid bodies. Moreover, the lipid profiling confirmed the accumulation of fatty acids derived from neutral and phospholipids in ypr147cΔ cells. Sequence analysis of Ypr147cp show the presence of an a/b hydrolase domain with the conserved GXSXG lipase motif. The YPR147c homology model was built and the modeled protein was analysed using RMSD and root mean square fluctuation (RMSF) for a 100 ns simulation trajectory. Docking the acetate, butyrate and palmitate ligands with the model confirmed covalent binding of ligands with the Ser207 of the GXSXG motif. Thus, Ypr147cp is a lipid droplet associated triacylglycerol lipase having short chain ester hydrolyzing capacity.

scholarly journals CIDE Proteins in Human Health and Disease

Cells ◽  
2019 ◽  
Vol 8 (3) ◽  
pp. 238 ◽  
Author(s):  
Mark Slayton ◽  
Abhishek Gupta ◽  
Bijinu Balakrishnan ◽  
Vishwajeet Puri
Keyword(s):  
Human Health ◽  
Dna Fragmentation ◽  
Lipid Droplet ◽  
Fat Metabolism ◽  
Physiological Role ◽  
Specific Protein ◽  
Metabolic Phenotype ◽  
Droplet Dynamics ◽  
Health And Disease ◽  
Cide Proteins

Cell death-Inducing DNA Fragmentation Factor Alpha (DFFA)-like Effector (CIDE) proteins have emerged as lipid droplet-associated proteins that regulate fat metabolism. There are three members in the CIDE protein family—CIDEA, CIDEB, and CIDEC (also known as fat-specific protein 27 (FSP27)). CIDEA and FSP27 are primarily expressed in adipose tissue, while CIDEB is expressed in the liver. Originally, based upon their homology with DNA fragmentation factors, these proteins were identified as apoptotic proteins. However, recent studies have changed the perception of these proteins, redefining them as regulators of lipid droplet dynamics and fat metabolism, which contribute to a healthy metabolic phenotype in humans. Despite various studies in humans and gene-targeting studies in mice, the physiological roles of CIDE proteins remains elusive. This review will summarize the known physiological role and metabolic pathways regulated by the CIDE proteins in human health and disease.

Exercise regulates lipid droplet dynamics in normal and fatty liver

2019 ◽  
Vol 1864 (12) ◽  
pp. 158519 ◽  
Author(s):  
Francisco Pino-de la Fuente ◽  
Laura Quezada ◽  
Carlos Sepúlveda ◽  
Matías Monsalves-Alvarez ◽  
Juan M. Rodríguez ◽  
...  
Keyword(s):  
Fatty Liver ◽  
Lipid Droplet ◽  
Droplet Dynamics

scholarly journals Lipid droplet dynamics at early stages ofMycobacterium marinuminfection inDictyostelium

2015 ◽  
Vol 17 (9) ◽  
pp. 1332-1349 ◽  
Author(s):  
Caroline Barisch ◽  
Peggy Paschke ◽  
Monica Hagedorn ◽  
Markus Maniak ◽  
Thierry Soldati
Keyword(s):  
Lipid Droplet ◽  
Droplet Dynamics ◽  
Early Stages

scholarly journals Seipin performs dissectible functions in promoting lipid droplet biogenesis and regulating droplet morphology

2015 ◽  
Vol 26 (4) ◽  
pp. 726-739 ◽  
Author(s):  
Bethany R. Cartwright ◽  
Derk D. Binns ◽  
Christopher L. Hilton ◽  
Sungwon Han ◽  
Qiang Gao ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Lipid Droplet ◽  
De Novo ◽  
Amino Terminus ◽  
Molecular Function ◽  
Null Mutant ◽  
Phospholipid Synthesis ◽  
Droplet Morphology ◽  
Size Heterogeneity

Seipin is necessary for both adipogenesis and lipid droplet (LD) organization in nonadipose tissues; however, its molecular function is incompletely understood. Phenotypes in the seipin-null mutant of Saccharomyces cerevisiae include aberrant droplet morphology (endoplasmic reticulum–droplet clusters and size heterogeneity) and sensitivity of droplet size to changes in phospholipid synthesis. It has not been clear, however, whether seipin acts in initiation of droplet synthesis or at a later step. Here we utilize a system of de novo droplet formation to show that the absence of seipin results in a delay in droplet appearance with concomitant accumulation of neutral lipid in membranes. We also demonstrate that seipin is required for vectorial budding of droplets toward the cytoplasm. Furthermore, we find that the normal rate of droplet initiation depends on 14 amino acids at the amino terminus of seipin, deletion of which results in fewer, larger droplets that are consistent with a delay in initiation but are otherwise normal in morphology. Importantly, other functions of seipin, namely vectorial budding and resistance to inositol, are retained in this mutant. We conclude that seipin has dissectible roles in both promoting early LD initiation and in regulating LD morphology, supporting its importance in LD biogenesis.

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