Publication

Malectin Participates in a Backup Glycoprotein Quality Control Pathway in the Mammalian ER

Related publications (28)

S-acylation and lipid exchange at the ER-Golgi membrane contact sites regulate pathogen entry in human cells

Cells have evolved endocytic pathways to internalize different molecules, to regulate intra-cellular communication and their interaction with external environment. Pathogens have co-evolved with cells to exploit these processes for infections. In particula ...

EPFL2024

Rescue of secretion of rare-disease-associated misfolded mutant glycoproteins in UGGT1 knock-out mammalian cells

Maurizio Molinari

Endoplasmic reticulum (ER) retention of misfolded glycoproteins is mediated by the ER-localized eukaryotic glycoprotein secretion checkpoint, UDP-glucose glycoprotein glucosyl-transferase (UGGT). The enzyme recognizes a misfolded glycoprotein and flags it ...

Wiley2024

Control of nuclear envelope dynamics during acute ER stress by LINC complexes disassembly and selective, asymmetric autophagy of the outer nuclear membrane

Maurizio Molinari

The endoplasmic reticulum (ER) extends to the outer (ONM) and the inner (INM) nuclear membrane forming the nuclear envelope (NE) that delimits the nucleoplasm containing the cell genome. Unfolded protein responses (UPRs) and reticulophagy responses increas ...

Taylor & Francis Inc2024

Golgi maturation-dependent glycoenzyme recycling controls glycosphingolipid biosynthesis and cell growth via GOLPH3

Anthony Vocat, Giovanni D'Angelo, Laura Capolupo, Riccardo Rizzo

Glycosphingolipids are important components of the plasma membrane where they modulate the activities of membrane proteins including signalling receptors. Glycosphingolipid synthesis relies on competing reactions catalysed by Golgi-resident enzymes during ...

WILEY2021

Enforced dimerization between XBP1s and ATF6f enhances the protective effects of the UPR in models of neurodegeneration

Hilal Lashuel, Sonia Donzelli

Alteration to endoplasmic reticulum (ER) proteostasis is observed in a variety of neurodegenerative diseases associated with abnormal protein aggregation. Activation of the unfolded protein response (UPR) enables an adaptive reaction to recover ER proteost ...

2021

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

Maurizio Molinari

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 ...

2020

Structural basis of Focal Adhesion Kinase activation on lipid membranes

Henning Paul-Julius Stahlberg, Frauke Gräter

Focal adhesion kinase (FAK) is a key component of the membrane proximal signaling layer in focal adhesion complexes, regulating important cellular processes, including cell migration, proliferation, and survival. In the cytosol, FAK adopts an autoinhibited ...

2020

Altered interplay between endoplasmic reticulum and mitochondria in Charcot-Marie-Tooth type 2A neuropathy

Bernard Schneider, Cylia Cloé Rochat, Mary-Claude Croisier-Coeytaux, Manisha Juneja, Omar El Mansour, Catherine Maclachlan, Roman Chrast, Nathalie Marie Géraldine Bernard

Mutations in the MFN2 gene encoding Mitofusin 2 lead to the development of Charcot-Marie-Tooth type 2A (CMT2A), a dominant axonal form of peripheral neuropathy. Mitofusin 2 is localized at both the outer membrane of mitochondria and the endoplasmic reticul ...

National Academy of Sciences2019

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

Lipid exchange and signaling at ER–Golgi contact sites

Meticulous observations of the cell perinuclear region where the Golgi and the endoplasmic reticulum (ER) networks intermingle have revealed close contact sites of barely 20 nm between these two organelles. Recent studies demonstrate that molecular machine ...

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

Single-Vesicle Assays Using Liposomes and Cell-Derived Vesicles: From Modeling Complex Membrane Processes to Synthetic Biology and Biomedical Applications

Horst Vogel, Horst Pick, Ana Catarina Rodrigues Alves

The plasma membrane is of central importance for defining the closed volume of cells in contradistinction to the extracellular environment. The plasma membrane not only serves as a boundary, but it also mediates the exchange of physical and chemical inform ...

AMER CHEMICAL SOC2018

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

Investigating the Biological Mechanisms underlying the Initiation of Autoimmunity against Beta Cell Antigens in Type 1 Diabetes

Chiara Cianciaruso

Type 1 diabetes (T1D) is an autoimmune disease characterized by circulating autoantibodies, lymphocytic infiltration of pancreatic islets of Langerhans, and cell-specific destruction of beta cells, leading to insulin deficiency and symptomatic hyperglycemi ...

EPFL2017

Aberrant Accumulation of the Diabetes Autoantigen GAD65 in Golgi Membranes in Conditions of ER Stress and Autoimmunity

Jeffrey Alan Hubbell, Miriella Carmela Pasquier, Steinunn Baekkeskov Hanahan, Edward Allen Phelps, Chiara Cianciaruso

Pancreatic islet β-cells are particularly susceptible to endoplasmic reticulum (ER) stress, which is implicated in β-cell dysfunction and loss during the pathogenesis of type 1 diabetes (T1D). The peripheral membrane protein GAD65 is an autoantigen in huma ...

Amer Diabetes Assoc2016

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

Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides

Maurizio Molinari

The endoplasmic reticulum (ER) is the site of maturation for secretory and membrane proteins in eukaryotic cells. The lumen of the mammalian ER contains >20 members of the protein disulfide isomerase (PDI) superfamily, which ensure formation of the correct ...

Amer Soc Cell Biology2015

How Viruses Hijack the ERAD Tuning Machinery

Maurizio Molinari, Riccardo Bernasconi

An essential step during the intracellular life cycle of many positive-strand RNA viruses is the rearrangement of host cell membranes to generate membrane-bound replication platforms. For example, Nidovirales and Flaviviridae subvert the membrane of the en ...

American Society for Microbiology2014

Proteostasis: Bad news and good news from the endoplasmic reticulum

Maurizio Molinari

The endoplasmic reticulum (ER) is an intracellular compartment dedicated to the synthesis and maturation of secretory and membrane proteins, totalling about 30% of the total eukaryotic cells proteome. The capacity to produce correctly folded polypeptides a ...

E M H Swiss Medical Publishers Ltd2014

The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease

Johan Auwerx, Laurent Mouchiroud, Virginija Jovaisaite

The ability to respond to various intracellular and/or extracellular stresses allows the organism to adapt to changing environmental conditions and drives evolution. It is now well accepted that a progressive decline of the efficiency of stress response pa ...

Company of Biologists2014