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

Biological Chemistry
Yutaka Suzuki, Manfred J Schmitt

Abstract

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 as cholera toxin, ricin or K28. According to the current view, disulfide-bonded proteins must either be reduced or rearranged to ensure translocation competence and entry into the cytosol from the ER. As the underlying mechanisms are still largely mysterious, we here focus on the redox status and disulfide isomerization of ERAD substrates and the role of oxidoreductases in the essential process of ER-to-cytosol retrotranslocation.

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Citations

Apr 10, 2015·Biological Chemistry·Johannes M HerrmannTobias P Dick
Jan 18, 2018·Arthritis & Rheumatology·Fatemeh NavidRobert A Colbert
Oct 20, 2018·Biological Reviews of the Cambridge Philosophical Society·Maria R DepaoliRoland Malli

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Methods Mentioned

BETA
lipidation
protein folding
transfection
ubiquitination
genetic modification

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