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      The endoplasmic reticulum and the unfolded protein response

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      Seminars in Cell & Developmental Biology

      Elsevier BV

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          Abstract

          The endoplasmic reticulum (ER) is the site where proteins enter the secretory pathway. Proteins are translocated into the ER lumen in an unfolded state and require protein chaperones and catalysts of protein folding to attain their final appropriate conformation. A sensitive surveillance mechanism exists to prevent misfolded proteins from transiting the secretory pathway and ensures that persistently misfolded proteins are directed towards a degradative pathway. In addition, those processes that prevent accumulation of unfolded proteins in the ER lumen are highly regulated by an intracellular signaling pathway known as the unfolded protein response (UPR). The UPR provides a mechanism by which cells can rapidly adapt to alterations in client protein-folding load in the ER lumen by expanding the capacity for protein folding. In addition, a variety of insults that disrupt protein folding in the ER lumen also activate the UPR. These include changes in intralumenal calcium, altered glycosylation, nutrient deprivation, pathogen infection, expression of folding-defective proteins, and changes in redox status. Persistent protein misfolding initiates apoptotic cascades that are now known to play fundamental roles in the pathogenesis of multiple human diseases including diabetes, atherosclerosis and neurodegenerative diseases.

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          Author and article information

          Journal
          Seminars in Cell & Developmental Biology
          Seminars in Cell & Developmental Biology
          Elsevier BV
          10849521
          December 2007
          December 2007
          : 18
          : 6
          : 716-731
          Article
          10.1016/j.semcdb.2007.09.003
          2706143
          18023214
          a972df47-ec2a-4e89-8e98-5c41736be173
          © 2007

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