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Protein Retention in the Endoplasmic Reticulum Mediated by GRP78

  • Andrew J. Dorner
  • Louise C. Wasley
  • Maryann G. Krane
  • Randal J. Kaufman
Conference paper
Part of the Serono Symposia, USA book series (SERONOSYMP)

Abstract

Proteins destined for secretion in mammalian cells transit the secretory pathway consisting of two major compartments: the endoplasmic reticulum (ER) and Golgi complex (GC) (Fig. 8.1). Proteins are first cotranslationally translocated into the lumen of the ER. The ER is the site of initial processing events that are crucial for proper folding of the nascent polypeptide. These processing events include signal peptide cleavage (1), addition of core N-linked oligosaccharides at consensus recognition sites (2), and disulfide bond formation mediated by protein disulfide isomerase (3). Attaining an appropriate conformation is essential for a protein to be efficiently transported from the ER to the GC (4). For most proteins, transport from the ER to the GC is the rate-limiting step for secretion (5, 6). This transport step requires ATP (7). Retention in the ER, and eventual degradation, is the fate of many secretion-incompetent proteins (8).

Keywords

Factor VIII Chinese Hamster Ovary Cell Golgi Complex Protein Disulfide Isomerase Glucose Regulate Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag New York, Inc. 1993

Authors and Affiliations

  • Andrew J. Dorner
  • Louise C. Wasley
  • Maryann G. Krane
  • Randal J. Kaufman

There are no affiliations available

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