Titlebook: Dislocation and Degradation of Proteins from the Endoplasmic Reticulum; Emmanuel Wiertz,Marjolein Kikkert Book 2005 The Editor(s) (if appl

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https://doi.org/10.1007/978-3-662-24970-3isfolding in the secretory pathway. Molecular chaperones and ER lumenal lectins are essential components of this process because they maintain the solubility of unfolded proteins and can target ERAD substrates to the cytoplasmic proteasome. Other factors are likely required to aid in the selection o

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https://doi.org/10.1007/978-3-662-24970-3own at present. This review provides an overview of ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s) with a role in the degradation of ER proteins. Their structure and functions are described, as well as their mutual interactions. Substrate specificity and functional redundancy of E3

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https://doi.org/10.1007/978-3-662-24970-3mical processes involving biosynthesis, degradation, translocation, intracellular transport, diffusion, and many more. Critical intermediates and end products of this cascade of events are peptides. The peptides are generated by the proteasome, degraded by peptidases unless transported into the ER w

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The Role of the Ubiquitination Machinery in Dislocation and Degradation of Endoplasmic Reticulum PrER proteins. Their structure and functions are described, as well as their mutual interactions. Substrate specificity and functional redundancy of E3 ligases are discussed, and other components of the ER degradation machinery that may associate with the ubiquitination system are reviewed.