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The Molecular Chaperones Interaction Networks in Protein Folding and Degradation pp 273–302Cite as

Chaperones of the Endoplasmic Reticulum Associated Degradation (ERAD) Pathway

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Part of the book series: Interactomics and Systems Biology ((INTERACTOM,volume 1))

Abstract

The endoplasmic reticulum (ER) is a diverse organelle with multiple specialized functions including the folding and assembly of secretory proteins. The ER harbors a number of chaperones, foldases, and covalent modifiers that aid in these processes. Due to the high protein throughput of the ER, inevitably some of the secreted proteins fail to reach their native state and therefore must be degraded. In a process known as ER-associated degradation (ERAD), misfolded proteins are recognized, translocated out of the ER into the cytoplasm, ubiquitinated, extracted from the ER membrane, deubiquitinated, and finally degraded by the 26S proteasome to prevent toxic build-up of non-native proteins. To account for the different properties and topologies of misfolded secretory cargo, a number of ER protein complexes are employed for the distinct steps of ERAD. Some of these complexes are shared between yeast and metazoan, while other appear unique to metazoa, reflecting their increased secretory load.

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  1. Department of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, MA, USA

    Johan C. Sunryd BS, Abla Tannous BS, MS, Lydia Lamriben BS & Daniel N. Hebert PhD

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  2. Abla Tannous BS, MS
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    Walid A. Houry

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Sunryd, J., Tannous, A., Lamriben, L., Hebert, D. (2014). Chaperones of the Endoplasmic Reticulum Associated Degradation (ERAD) Pathway. In: Houry, W. (eds) The Molecular Chaperones Interaction Networks in Protein Folding and Degradation. Interactomics and Systems Biology, vol 1. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-1130-1_11

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