Role of EDEM in the Release of Misfolded Glycoproteins from the Calnexin Cycle

DOI Web Site 被引用文献34件
  • Maurizio Molinari
    Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland.
  • Verena Calanca
    Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland.
  • Carmela Galli
    Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland.
  • Paola Lucca
    Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland.
  • Paolo Paganetti
    Nervous System, Novartis Pharma AG, CH-4002 Basel, Switzerland.

抄録

<jats:p>The mechanisms that determine how folding attempts are interrupted to target folding-incompetent proteins for endoplasmic reticulum–associated degradation (ERAD) are poorly defined. Here the α-mannosidase I–like protein EDEM was shown to extract misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. EDEM overexpression resulted in faster release of folding-incompetent proteins from the calnexin cycle and earlier onset of degradation, whereas EDEM down-regulation prolonged folding attempts and delayed ERAD. Up-regulation of EDEM during ER stress may promote cell recovery by clearing the calnexin cycle and by accelerating ERAD of terminally misfolded polypeptides.</jats:p>

収録刊行物

  • Science

    Science 299 (5611), 1397-1400, 2003-02-28

    American Association for the Advancement of Science (AAAS)

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