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      One step at a time: endoplasmic reticulum-associated degradation.

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          Abstract

          Protein folding in the endoplasmic reticulum (ER) is monitored by ER quality control (ERQC) mechanisms. Proteins that pass ERQC criteria traffic to their final destinations through the secretory pathway, whereas non-native and unassembled subunits of multimeric proteins are degraded by the ER-associated degradation (ERAD) pathway. During ERAD, molecular chaperones and associated factors recognize and target substrates for retrotranslocation to the cytoplasm, where they are degraded by the ubiquitin-proteasome machinery. The discovery of diseases that are associated with ERAD substrates highlights the importance of this pathway. Here, we summarize our current understanding of each step during ERAD, with emphasis on the factors that catalyse distinct activities.

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          Author and article information

          Journal
          Nat Rev Mol Cell Biol
          Nature reviews. Molecular cell biology
          Springer Science and Business Media LLC
          1471-0080
          1471-0072
          Dec 2008
          : 9
          : 12
          Affiliations
          [1 ] Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
          Article
          nrm2546 NIHMS96696
          10.1038/nrm2546
          2654601
          19002207
          477f4e68-8a94-4266-8521-f2bf8251d695
          History

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