scholarly journals Identification and Characterization of Associated with Lipid Droplet Protein 1: A Novel Membrane-Associated Protein That Resides on Hepatic Lipid Droplets

Traffic ◽  
2006 ◽  
Vol 7 (9) ◽  
pp. 1254-1269 ◽  
Author(s):  
Silvia Turró ◽  
Mercedes Ingelmo-Torres ◽  
Josep M. Estanyol ◽  
Francesc Tebar ◽  
Manuel A. Fernández ◽  
...  
Keyword(s):  
Lipid Droplet ◽  
Lipid Droplets ◽  
Hepatic Lipid ◽  
Identification And Characterization ◽  
Lipid Droplet Protein

Identification of Perilipin-2 as a lipid droplet protein regulated in oocytes during maturation

2010 ◽  
Vol 22 (8) ◽  
pp. 1262 ◽  
Author(s):  
Xing Yang ◽  
Kylie R. Dunning ◽  
Linda L.-Y. Wu ◽  
Theresa E. Hickey ◽  
Robert J. Norman ◽  
...  
Keyword(s):  
Lipid Droplet ◽  
Lipid Content ◽  
Lipid Droplets ◽  
Intracellular Lipids ◽  
Epidermal Growth ◽  
Novel Method ◽  
Perilipin 2 ◽  
Lipid Droplet Protein

Lipid droplet proteins regulate the storage and utilisation of intracellular lipids. Evidence is emerging that oocyte lipid utilisation impacts embryo development, but lipid droplet proteins have not been studied in oocytes. The aim of the present study was to characterise the size and localisation of lipid droplets in mouse oocytes during the periovulatory period and to identify lipid droplet proteins as potential biomarkers of oocyte lipid content. Oocyte lipid droplets, visualised using a novel method of staining cumulus–oocyte complexes (COCs) with BODIPY 493/503, were small and diffuse in oocytes of preovulatory COCs, but larger and more centrally located after maturation in response to ovulatory human chorionic gonadotrophin (hCG) in vivo, or FSH + epidermal growth factor in vitro. Lipid droplet proteins Perilipin, Perilipin-2, cell death-inducing DNA fragmentation factor 45-like effector (CIDE)-A and CIDE-B were detected in the mouse ovary by immunohistochemistry, but only Perilipin-2 was associated with lipid droplets in the oocyte. In COCs, Perilipin-2 mRNA and protein increased in response to ovulatory hCG. IVM failed to induce Perilipin-2 mRNA, yet oocyte lipid content was increased in this context, indicating that Perilipin-2 is not necessarily reflective of relative oocyte lipid content. Thus, Perilipin-2 is a lipid droplet protein in oocytes and its induction in the COC concurrent with dynamic reorganisation of lipid droplets suggests marked changes in lipid utilisation during oocyte maturation.

scholarly journals Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets

2012 ◽  
Vol 23 (5) ◽  
pp. 896-909 ◽  
Author(s):  
Anoop Kumar G. Velikkakath ◽  
Taki Nishimura ◽  
Eiko Oita ◽  
Naotada Ishihara ◽  
Noboru Mizushima
Keyword(s):  
Lipid Droplet ◽  
Lipid Droplets ◽  
Autophagic Flux ◽  
Autophagosome Formation ◽  
Independent Manner ◽  
Intracellular Degradation ◽  
Atg Proteins ◽  
High Conservation ◽  
Droplet Morphology

Macroautophagy is an intracellular degradation system by which cytoplasmic materials are enclosed by the autophagosome and delivered to the lysosome. Autophagosome formation is considered to take place on the endoplasmic reticulum and involves functions of autophagy-related (Atg) proteins. Here, we report the identification and characterization of mammalian Atg2 homologues Atg2A and Atg2B. Simultaneous silencing of Atg2A and Atg2B causes a block in autophagic flux and accumulation of unclosed autophagic structures containing most Atg proteins. Atg2A localizes on the autophagic membrane, as well as on the surface of lipid droplets. The Atg2A region containing amino acids 1723–1829, which shows relatively high conservation among species, is required for localization to both the autophagic membrane and lipid droplet and is also essential for autophagy. Depletion of both Atg2A and Atg2B causes clustering of enlarged lipid droplets in an autophagy-independent manner. These data suggest that mammalian Atg2 proteins function both in autophagosome formation and regulation of lipid droplet morphology and dispersion.

scholarly journals A mycobacterial glycine-rich protein governs actin-based motility

2021 ◽  
Author(s):  
Norbert S. Hill ◽  
Matthew D. Welch
Keyword(s):  
Lipid Droplet ◽  
Actin Polymerization ◽  
Close Relative ◽  
Bacterial Surface ◽  
Motility Factor ◽  
New Class ◽  
Intracellular Movement ◽  
Mycobacterial Pathogenesis ◽  
Identification And Characterization

Mycobacterium marinum, a close relative of the significant human pathogen Mycobacterium tuberculosis, polymerizes host actin at the bacterial surface to drive intracellular movement and cell-to-cell spread during infection. Here, we report the identification and characterization of MirA, the M. marinum actin-based motility factor. MirA is a member of the glycine-rich PE_PGRS family of ESX-5-secreted proteins. MirA uses an amphipathic helix to anchor into the mycobacterial outer membrane and, surprisingly, also the surface of host lipid droplet organelles. The glycine-rich PGRS domain in MirA directly binds and activates host N-WASP to stimulate actin polymerization through the Arp2/3 complex, directing both bacterial and lipid droplet actin-based motility. MirA is dissimilar to known N-WASP activating ligands and may represent a new class of microbial and host actin regulator. Additionally, the MirA-N-WASP interaction represents a model to understand how the enigmatic PE_PGRS proteins contribute to mycobacterial pathogenesis.

scholarly journals RNA Interference Silencing of a Major Lipid Droplet Protein Affects Lipid Droplet Size in Chlamydomonas reinhardtii

2009 ◽  
Vol 9 (1) ◽  
pp. 97-106 ◽  
Author(s):  
Eric R. Moellering ◽  
Christoph Benning
Keyword(s):  
Rna Interference ◽  
Chlamydomonas Reinhardtii ◽  
Droplet Size ◽  
Lipid Droplet ◽  
Lipid Droplets ◽  
Biofuel Production ◽  
Nitrogen Deprivation ◽  
Green Algal ◽  
Lipid Droplet Size ◽  
Lipid Droplet Protein

ABSTRACT Eukaryotic cells store oils in the chemical form of triacylglycerols in distinct organelles, often called lipid droplets. These dynamic storage compartments have been intensely studied in the context of human health and also in plants as a source of vegetable oils for human consumption and for chemical or biofuel feedstocks. Many microalgae accumulate oils, particularly under conditions limiting to growth, and thus have gained renewed attention as a potentially sustainable feedstock for biofuel production. However, little is currently known at the cellular or molecular levels with regard to oil accumulation in microalgae, and the structural proteins and enzymes involved in the biogenesis, maintenance, and degradation of algal oil storage compartments are not well studied. Focusing on the model green alga Chlamydomonas reinhardtii, the accumulation of triacylglycerols and the formation of lipid droplets during nitrogen deprivation were investigated. Mass spectrometry identified 259 proteins in a lipid droplet-enriched fraction, among them a major protein, tentatively designated major lipid droplet protein (MLDP). This protein is specific to the green algal lineage of photosynthetic organisms. Repression of MLDP gene expression using an RNA interference approach led to increased lipid droplet size, but no change in triacylglycerol content or metabolism was observed.

scholarly journals Identification and Characterization of Human Norovirus NTPase Regions Required for Lipid Droplet Localization, Cellular Apoptosis, and Interaction with the Viral P22 Protein

2021 ◽  
Author(s):  
Ju-Bei Yen ◽  
Lee-Wen Chen ◽  
Ling-Huei Wei ◽  
Chien-Hui Hung ◽  
Shie-Shan Wang ◽  
...  
Keyword(s):  
Cell Culture ◽  
Lipid Droplet ◽  
Culture System ◽  
Host Cells ◽  
Cell Culture System ◽  
Human Norovirus ◽  
Efficient Cell Culture System ◽  
Cellular Apoptosis ◽  
Identification And Characterization

Human noroviruses (HuNVs) are the major agent of global gastroenteritis outbreaks. However, due to the lack of an efficient cell culture system for HuNV propagation, functions of the viral-encoded proteins in host cells are still poorly understood.

scholarly journals Characterization of a lipid droplet protein from Yarrowia lipolytica that is required for its oleaginous phenotype

2018 ◽  
Vol 1863 (10) ◽  
pp. 1193-1205 ◽  
Author(s):  
Govindprasad Bhutada ◽  
Martin Kavšček ◽  
Florian Hofer ◽  
Gabriela Gogg-Fassolter ◽  
Martina Schweiger ◽  
...  
Keyword(s):  
Yarrowia Lipolytica ◽  
Lipid Droplet ◽  
Lipid Droplet Protein
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