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Maurizio Molinari

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Related publications (57)

Endoplasmic Reticulum and Lysosomal Quality Control of Four Nonsense Mutants of Iduronate 2-Sulfatase Linked to Hunter's Syndrome

Maurizio Molinari, Andrea Cavalli

Hunter's syndrome (mucopolysaccharidosis type II) is a rare X-linked lysosomal storage disorder caused by mutations in the iduronate-2-sulfatase (IDS) gene. Motivated by the case of a child affected by this syndrome, we compared the intracellular fate of w ...

2020

Proteasomal and lysosomal clearance of faulty secretory proteins: ER-associated degradation (ERAD) and ER-to-lysosome-associated degradation (ERLAD) pathways

Maurizio Molinari

About 40% of the eukaryotic cell's proteins are inserted co- or post-translationally in the endoplasmic reticulum (ER), where they attain the native structure under the assistance of resident molecular chaperones and folding enzymes. Subsequently, these pr ...

2019

Schwann cells ER-associated degradation contributes to myelin maintenance in adult nerves and limits demyelination in CMT1B mice

Maurizio Molinari, Francesca Bianchi

In the peripheral nervous system (PNS) myelinating Schwann cells synthesize large amounts of myelin protein zero (P0) glycoprotein, an abundant component of peripheral nerve myelin. In humans, mutations in P0 cause the demyelinating Charcot-Marie-Tooth 1B ...

2019

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

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

A selective ER‐phagy exerts procollagen quality control via a Calnexin‐FAM134B complex

Maurizio Molinari

Autophagy is a cytosolic quality control process that recognizessubstrates through receptor-mediated mechanisms. Procollagens,the most abundant gene products in Metazoa, are synthesized inthe endoplasmic reticulum (ER), and a fraction that fails to attaint ...

2018

Chemical stresses fail to mimic the unfolded protein response resulting from luminal load with unfolded polypeptides

Maurizio Molinari

2018

Eat it right: ER-phagy and recovER-phagy

Maurizio Molinari

Portland Press Ltd2018

The reductase TMX1 contributes to ERAD by preferentially acting on membrane-associated folding-defective polypeptides

Maurizio Molinari

2018

Role of SEC62 in ER maintenance: A link with ER stress tolerance in SEC62-overexpressing tumors?

Maurizio Molinari

Amplification of the candidate oncogene TLOC1/SEC62 in tumors correlates with reduced patient survival. The recently reported role of SEC62 as an autophagy receptor that controls endoplasmic reticulum (ER) size and function might open new scenarios for und ...

Taylor & Francis Inc2017

Quality control mechanisms of protein biogenesis: proteostasis dies hard

Maurizio Molinari

The biosynthesis of proteins entails a complex series of chemical reactions that transform the information stored in the nucleic acid sequence into a polypeptide chain that needs to properly fold and reach its functional location in or outside the cell. It ...

Amer Inst Mathematical Sciences-Aims2016

Five Questions (with their Answers) on ER-Associated Degradation

Maurizio Molinari

Production of a functional proteome is a major burden for our cells. Native proteins operate inside and outside the cells to eventually warrant life and adaptation to metabolic and environmental changes, there is no doubt that production and inappropriate ...

Wiley-Blackwell2016

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

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Nicolas Dupont, Françoise Gisou van der Goot Grunberg, Li Jin, Lionel Blanc, Andreas Kern, Andreas Mayer, Yin Chen, Darren Moore, Maurizio Molinari, Xu Liu, Jun Ren, Ziwei Qu, Li Yu, Xin Qi, Paolo Paganetti, Wei Chen, Peiwen Chen, Jian Zhang, Hong Jiang, Bo Wang, Yi Sun, Rakesh Kumar, Qi Chen, Si Chen, Ke Liu, Feng Xu, Qing Zhong, Hua Bai, Yang Sun, Sheng Li, Wei Liu, Peng Wang, Zhen Yan, Bo Liu, Fan Zhang, Jian Wu, Jian Wang, Li Zhang, Chih-Peng Chang, Giuseppe Russo, Sandra Moreno, Ying Jiang, Hong Zhang, Liang Xu, , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , ,

A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residue

Maurizio Molinari

Only native polypeptides are released from the endoplasmic reticulum (ER) to be transported at the site of activity. Persistently misfolded proteins are retained and eventually selected for ER-associated degradation (ERAD). The paradox of a structure-based ...

Amer Soc Cell Biology2015

The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein

Maurizio Molinari

Although the accumulation of a misfolded and protease-resistant form of the prion protein (PrP) is a key event in prion pathogenesis, the cellular factors involved in its folding and quality control are poorly understood. PrP is a glycosylated and disulfid ...

Amer Soc Biochemistry Molecular Biology Inc2015

N-linked sugar-regulated protein folding and quality control in the ER

Maurizio Molinari

Asparagine-linked glycans (N-glycans) are displayed on the majority of proteins synthesized in the endoplasmic reticulum (ER). Removal of the outermost glucose residue recruits the lectin chaperone malectin possibly involved in a first triage of defective ...

Academic Press Ltd- Elsevier Science Ltd2015

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 (vol 88, pg 10272, 2014)

Maurizio Molinari, Riccardo Bernasconi

American Society for Microbiology2015

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

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Taylor & Francis Inc2016