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    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

    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

    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...