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Retro-Translocation of Proteins Across the Endoplasmic Reticulum Membrane

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Protein Movement Across Membranes

Part of the book series: Molecular Biology Intelligence Unit ((MBIU))

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Abstract

Many proteins synthesised in the cytosol are translocated across or inserted into the endoplasmic reticulum (ER) membrane. These proteins include not only those resident in the ER itself, but others destined for post-ER destinations such as the Golgi complex, lysosomes or secretion into the extracellular environment. Proteins that fail to fold or assemble correctly are detected by the quality control system of the ER and are disposed of by a process known as ER-associated degradation. Degradation does not occur in the ER itself. Rather the aberrant proteins are exported from the ER for degradation by the ubiquitin/proteasome pathway in the cytosol. This involves the retro-translocation of these proteins across the ER membrane. In this chapter we discuss our current understanding of the process of retro-translocation.

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  1. Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK

    J. Michael Lord & Lynne M. Roberts

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  1. J. Michael Lord
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Correspondence to J. Michael Lord .

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Lord, J.M., Roberts, L.M. (2005). Retro-Translocation of Proteins Across the Endoplasmic Reticulum Membrane. In: Protein Movement Across Membranes. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/0-387-30871-7_7

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