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Université de Fribourg

Seipin accumulates and traps diacylglycerols and triglycerides in its ring-like structure

Zoni, Valeria ; Khaddaj, Rasha ; Lukmantara, Ivan ; Shinoda, Wataru ; Hongyuan, Yang ; Schneiter, Roger ; Vanni, Stefano

In: Proceedings of the National Academy of Sciences, 2021, vol. 118, no. 10, p. e2017205118

Lipid droplets (LDs) are intracellular organelles responsible for lipid storage, and they emerge from the endoplasmic reticulum (ER) upon the accumulation of neutral lipids, mostly triglycerides (TG), between the two leaflets of the ER membrane. LD biogenesis takes place at ER sites that are marked by the protein seipin, which subsequently recruits additional proteins to catalyze LD formation....

Université de Fribourg

Raft-like lipid microdomains drive autophagy initiation via AMBRA1-ERLIN1 molecular association within MAMs

Manganelli, Valeria ; Matarrese, Paola ; Antonioli, Manuela ; Gambardella, Lucrezia ; Vescovo, Tiziana ; Gretzmeier, Christine ; Longo, Agostina ; Capozzi, Antonella ; Recalchi, Serena ; Riitano, Gloria ; Misasi, Roberta ; Dengjel, Jörn ; Malorni, Walter ; Fimia, Gian Maria ; Sorice, Maurizio ; Garofalo, Tina

In: Autophagy, 2020, p. 1-21

Mitochondria-associated membranes (MAMs) are essential communication subdomains of the endoplasmic reticulum (ER) that interact with mitochondria. We previously demonstrated that, upon macroautophagy/autophagy induction, AMBRA1 is recruited to the BECN1 complex and relocalizes to MAMs, where it regulates autophagy by interacting with raft-like components. ERLIN1 is an endoplasmic reticulum...

Università della Svizzera italiana

Thioredoxin-related transmembrane proteins : TMX1 and little brothers TMX2, TMX3, TMX4 and TMX5

Guerra, Concetta ; Molinari, Maurizio

In: Cells, 2020, vol. 9, no. 9, p. 11 p

The endoplasmic reticulum (ER) is site of synthesis and maturation of membrane and secretory proteins in eukaryotic cells. The ER contains more than 20 members of the Protein Disulfide Isomerase (PDI) family. These enzymes regulate formation, isomerization and disassembly of covalent bonds between cysteine residues. As such, PDIs ensure protein folding, which is required to attain functional...

Université de Fribourg

From zero to six double bonds: phospholipid unsaturation and organelle function

Antonny, Bruno ; Vanni, Stefano ; Shindou, Hideo ; Thierry, Ferreira

In: Trends in Cell Biology, 2015, vol. 25, no. 7, p. 427–436

Cellular phospholipids (PLs) differ by the nature of their polar heads as well as by the length and unsaturation level of their fatty acyl chains. We discuss how the ratio between saturated, monounsaturated, and polyunsaturated PLs impacts on the functions of such organelles as the endoplasmic reticulum, synaptic vesicles, and photoreceptor discs. Recent experiments and simulations suggest...

Université de Fribourg

Lipid droplet biogenesis from specialized ER subdomains

Choudhary, Vineet ; Schneiter, Roger

In: Microbial Cell, 2020, vol. 7, no. 8, p. 218–221

Lipid droplets (LDs) are cellular compartments dedicated to the storage of metabolic energy in the form of neutral lipids, commonly known as “fat”. The biogenesis of LDs takes place in the endoplasmic reticulum (ER), but its spatial and temporal organization is poorly understood. How exactly sites of LD formation are selected and the succession of proteins and lipids needed to mediate...

Université de Fribourg

Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid droplet biogenesis

Choudhary, Vineet ; El Atab, Ola ; Mizzon, Giulia ; Prinz, William A. ; Schneiter, Roger

In: Journal of Cell Biology, 2020, vol. 219, no. 7, p. -

Lipid droplets (LDs) are fat storage organelles that originate from the endoplasmic reticulum (ER). Relatively little is known about how sites of LD formation are selected and which proteins/lipids are necessary for the process. Here, we show that LDs induced by the yeast triacylglycerol (TAG)-synthases Lro1 and Dga1 are formed at discrete ER subdomains defined by seipin (Fld1), and a...