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Università della Svizzera italiana

Endoplasmic reticulum turnover : ER-phagy and other flavors in selective and non-selective ER clearance

Fregno, Ilaria ; Molinari, Maurizio

In: F1000Research, 2018, vol. 7, p. 454

The endoplasmic reticulum (ER) is a highly dynamic organelle in eukaryotic cells. It is deputed to lipid and protein biosynthesis, calcium storage, and the detoxification of various exogenous and endogenous harmful compounds. ER activity and size must be adapted rapidly to environmental and developmental conditions or biosynthetic demand. This is achieved on induction of thoroughly studied...

Università della Svizzera italiana

Unconventional use of LC3 by coronaviruses through the alleged subversion of the ERAD tuning pathway

Reggiori, Fulvio ; De Haan, Cornelis A.M. ; Molinari, Maurizio

In: Viruses, 2011, vol. 3, no. 9, p. 1610-1623

Pathogens of bacterial and viral origin hijack pathways operating in eukaryotic cells in many ways in order to gain access into the host, to establish themselves and to eventually produce their progeny. The detailed molecular characterization of the subversion mechanisms devised by pathogens to infect host cells is crucial to generate targets for therapeutic intervention. Here we review recent...

Università della Svizzera italiana

Chronic delivery of antibody fragments using immunoisolated cell implants as a passive vaccination tool

Belaunzaran, Osiris Marroquin ; Cordero, Maria Isabel ; Setola, Veronica ; Bianchi, Siro ; Galli, Carmela ; Bouche, Nicolas ; Mlynarik, Vladimir ; Gruetter, Rolf ; Sandi, Carmen ; Bensadoun, Jean-Charles ; Molinari, Maurizio ; Aebischer, Patrick

In: Plos one, 2011, vol. 6, no. 4, p. e18268

Background: Monoclonal antibodies and antibody fragments are powerful biotherapeutics for various debilitating diseases. However, high production costs, functional limitations such as inadequate pharmacokinetics and tissue accessibility are the current principal disadvantages for broadening their use in clinic. Methodology and Principal Findings: We report a novel method for the long-term ...

Università della Svizzera italiana

Malectin participates in a backup glycoprotein quality control pathway in the mammalian ER

Galli, Carmela ; Bernasconi, Riccardo ; Soldà, Tatiana ; Calanca, Verena ; Molinari, Maurizio

In: Plos one, 2011, vol. 6, no. 1, p. e16304

Malectin is a conserved, endoplasmic reticulum (ER)-resident lectin that recognizes high mannose oligosaccharides displaying terminal glucose residues. Here we show that Malectin is an ER stress-induced protein that selectively associates with glycopolypeptides without affecting their entry and their retention in the Calnexin chaperone system. Analysis of the obligate Calnexin client...

Università della Svizzera italiana

Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation

Bernasconi, Riccardo ; Soldà, Tatiana ; Galli, Carmela ; Pertel, Thomas ; Luban, Jeremy ; Molinari, Maurizio

In: Plos one, 2010, vol. 5, no. 9, p. e13008

Peptidyl-prolyl cis/trans isomerases (PPIs) catalyze cis/trans isomerization of peptide bonds preceding proline residues. The involvement of PPI family members in protein refolding has been established in test tube experiments. Surprisingly, however, no data is available on the involvement of endoplasmic reticulum (ER)-resident members of the PPI family in protein folding, quality control or...

Università della Svizzera italiana

The protein disulfide isomerase ERp57 regulates the steady-state levels of the prion protein

Torres, Mauricio ; Medinas,Danilo B. ; Matamala, José Manuel ; Woehlbier, Ute ; Cornejo, Víctor Hugo ; Solda, Tatiana ; Andreu, Catherine ; Rozas, Pablo ; Matus, Soledad ; Muñoz, Natalia ; Vergara, Carmen ; Cartier, Luis ; Soto, Claudio ; Molinari, Maurizio ; Hetz, Claudio

In: The journal of biological chemistry, 2015, vol. 290, no. 39, p. 23631-23645

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 disulfide-bonded protein synthesized at the endoplasmic reticulum (ER). The ER foldase ERp57 (also known as Grp58) is highly expressed in the brain...

Università della Svizzera italiana

How viruses hijack the ERAD tuning machinery

Noack, Julia ; Bernasconi, Riccardo ; Molinari, Maurizio

In: Journal of virology, 2014, vol. 88, no. 18, p. 10272-10275

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 endoplasmic reticulum (ER) for their replication. However, the absence of conventional ER and secretory pathway markers in virus-induced...

Università della Svizzera italiana

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

Brambilla Pisoni, Giorgia ; Ruddock, Lloyd W. ; Bulleid, Neil ; Molinari, Maurizio

In: Molecular biology of the cell, 2015, vol. 26, no. 19, p. 3373-3556

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 set of intramolecular and intermolecular disulfide bonds as crucial, rate-limiting reactions of the protein folding process. Components of...

Università della Svizzera italiana

UDP-glucose : glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum

Ferris, Sean P. ; Jaber, Nikita S. ; Molinari, Maurizio ; Arvan, Peter ; Kaufman, Randal J.

In: Molecular biology of the cell, 2013, vol. 24, no. 17, p. 2597-2608

Protein folding in the endoplasmic reticulum (ER) is error prone, and ER quality control (ERQC) processes ensure that only correctly folded proteins are exported from the ER. Glycoproteins can be retained in the ER by ERQC, and this retention contributes to multiple human diseases, termed ER storage diseases. UDP- glucose:glycoprotein glucosyltransferase (UGGT1) acts as a central component of...

Università della Svizzera italiana

Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates

Bernasconi, Riccardo ; Galli, Carmela ; Calanca, Verena ; Nakajima, Toshihiro ; Molinari, Maurizio

In: The journal of cell biology, 2010, vol. 188, no. 2, p. 223–235

Sophisticated quality control mechanisms prolong retention of protein-folding intermediates in the endoplasmic reticulum (ER) until maturation while sorting out terminally misfolded polypeptides for ER-associated degradation (ERAD). The presence of structural lesions in the luminal, transmembrane, or cytosolic domains determines the classification of misfolded polypeptides as ERAD-L, -M, or -C...