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Thioredoxin-Related Transmembrane Proteins: TMX1 and Little Brothers TMX2, TMX3, TMX4 and TMX5

Publications associées (67)

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ER-to-lysosome-associated degradation of proteasome-resistant ATZ polymers occurs via receptor-mediated vesicular transport

Maurizio Molinari, Paolo Paganetti

Maintenance of cellular proteostasis relies on efficient clearance of defective gene products. For misfolded secretory proteins, this involves dislocation from the endoplasmic reticulum (ER) into the cytosol followed by proteasomal degradation. However, po ...

2018

Three branches to rule them all? UPR signalling in response to chemically versus misfolded proteins-induced ER stress

Maurizio Molinari

Study of the unfolded protein responses (UPR) is mainly addressed by challenging eukaryotic cells with chemical compounds that impair calcium, redox or glycan homeostasis. These dramatically alter the endoplasmic reticulum (ER) environment and function, bu ...

2018

Glycosphingolipid metabolism in cell fate specification

Giovanni D'Angelo, Laura Capolupo, Jaipreet Singh Loomba

Glycosphingolipids (GSLs) are ubiquitous components of eukaryotic plasma membranes that consist of a ceramide backbone linked to a glycan moiety. Both the ceramide and the glycan parts of GSLs display structural variations that result in a remarkable reper ...

2018

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We report systematic transmission electron microscope (TEM) observations of the cellular ultrastructure of selected, small rotalid benthic foraminifera. Nine species from different environments (intertidal mudflat, fjord, and basin) were investigated: Ammo ...

2018

Realistic models of cellular environments have long captured the imagination of biologists and physical scientists. More than 20 years ago, Goodshellâs inspiring rendering of cellular environments provided the foundation for the idea of capturing the ful ...

EPFL2017

Regulation of Endoplasmic Reticulum Architecture by Protein S-Palmitoylation

Patrick Alain Sandoz

The endoplasmic reticulum (ER) is the largest organelle in mammalian cells. More than 50 years ago, its morphology was already described as consisting of two major compartments: the rough ER and the smooth ER, which both fulfil precise and distinct functio ...

EPFL2017

Polymer nanomedicines are very attractive to improve the delivery of chemotherapeutics. Polymer conjugates and other polymer-based nanocarriers allow to increase plasma half-life and drug bioavailability and can also be guided toward tumors using passive a ...

2017

Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery

Maurizio Molinari

The endoplasmic reticulum (ER) is a site of protein biogenesis in eukaryotic cells. Perturbing ER homeostasis activates stress programs collectively called the unfolded protein response (UPR). The UPR enhances production of ER-resident chaperones and enzym ...

Nature Publishing Group2016

Ubiquitin-dependent folding of the Wnt signaling coreceptor LRP6

Françoise Gisou van der Goot Grunberg, Laurence Gouzi Abrami, Béatrice Kunz, Michal Feldman Elmalam, Elsa Anne Perrody

Many membrane proteins fold inefficiently and require the help of enzymes and chaperones. Here we reveal a novel folding assistance system that operates on membrane proteins from the cytosolic side of the endoplasmic reticulum (ER). We show that folding of ...

Elife Sciences Publications Ltd2016

A molecular chaperone dedicated to folding and translocation of reductive dehalogenases

Julien Maillard, Corantin Grob

Reductive dehalogenases (rdhA, RDases) are key enzymes involved in anaerobic organohalide respiration (OHR), during which bacteria are able to use chlorinated compounds as terminal electron acceptors. RDases are redox enzymes containing FeS clusters and a ...

2016