Retrotranslocation: Endoplasmic Reticulum’s Junk Disposal Mechanism

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4SCIENTIFIC REVIEW Retrotranslocation: Endoplasmic Reticulum’s Junk Disposal Mechanism

The primary structure of polypeptides is converted to their final tertiary and quaternary structure by sequential maturation steps, and the endoplasmic reticulum (ER) provides the environment for the polypeptides to attain their proper 3-dimensional architecture. Proteins that misfold or fail to oligomerize with their partners (Chen et al., 1998; Wileman et al., 1990) are quickly degraded, as u...

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How ricin and Shiga toxin reach the cytosol of target cells: retrotranslocation from the endoplasmic reticulum.

A number of protein toxins bind at the surface of mammalian cells and after endocytosis traffic to the endoplasmic reticulum, where the toxic A chains are liberated from the holotoxin. The free A chains are then dislocated, or retrotranslocated, across the ER membrane into the cytosol. Here, in contrast to ER substrates destined for proteasomal destruction, they undergo folding to a catalytic c...

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Redox diversity in ERAD-mediated protein retrotranslocation from the endoplasmic reticulum: a complex puzzle.

Misfolded and incorrectly assembled proteins in the secretory pathway are eliminated by ubiquitylation and proteasomal degradation in a process known as ER-associated degradation (ERAD). Retrotranslocation of diverse substrates including misfolded proteins and viruses occurs through channels in the ER membrane, which are also utilized for host cell penetration by A/B class protein toxins such a...

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Retrotranslocation of prion proteins from the endoplasmic reticulum by preventing GPI signal transamidation.

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ژورنال

عنوان ژورنال: Einstein Journal of Biology and Medicine

سال: 2016

ISSN: 1559-5498,1559-5501

DOI: 10.23861/ejbm200421444