Updates on “Endoplasmic Reticulum Redox”
نویسندگان
چکیده
منابع مشابه
FORUM EDITORIAL Updates on ‘‘Endoplasmic Reticulum Redox’’
Probably the most important message that a Forum on the reduction–oxidation (redox) environment in the endoplasmic reticulum (ER) must nowadays convey is that an ‘‘ER redox state’’ as such does not exist. The ER rather features a variety of redox systems, which—in many cases—react independently with incoming substrates and xenobiotics. Thus, any statement claiming ER hyperor hypo-oxidation unde...
متن کاملEndoplasmic reticulum-dependent redox reactions control endoplasmic reticulum-associated degradation and pathogen entry.
SIGNIFICANCE Protein misfolding within the endoplasmic reticulum (ER) is managed by an ER quality control system that retro-translocates aberrant proteins into the cytosol for proteasomal destruction. This process, known as ER-associated degradation, utilizes the action of ER redox enzymes to accommodate the disulfide-bonded nature of misfolded proteins. Strikingly, various pathogenic viruses a...
متن کاملEro1 and redox homeostasis in the endoplasmic reticulum.
Living cells must be able to respond to physiological and environmental fluctuations that threaten cell function and viability. A cellular event prone to disruption by a wide variety of internal and external perturbations is protein folding. To ensure protein folding can proceed under a range of conditions, the cell has evolved transcriptional, translational, and posttranslational signaling pat...
متن کاملGreen fluorescent protein-based monitoring of endoplasmic reticulum redox poise
Pathological endoplasmic reticulum (ER) stress is tightly linked to the accumulation of reactive oxidants, which can be both upstream and downstream of ER stress. Accordingly, detrimental intracellular stress signals are amplified through establishment of a vicious cycle. An increasing number of human diseases are characterized by tissue atrophy in response to ER stress and oxidative injury. Ex...
متن کاملProtein folding: A missing redox link in the endoplasmic reticulum
Native disulphide-bond formation during protein folding in the endoplasmic reticulum requires oxidative machinery, the components and mechanism of which are not yet fully understood. Two recent papers have identified a novel protein component that appears to play a key role in this important redox pathway.
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ژورنال
عنوان ژورنال: Antioxidants & Redox Signaling
سال: 2012
ISSN: 1523-0864,1557-7716
DOI: 10.1089/ars.2011.4463