Mechanism and components of endoplasmic reticulum-associated degradation [PDF]
Journal of Biochemistry, 2009 The folding of secretory and membrane proteins takes place in the endoplasmic reticulum (ER). The quality of the proteins folded in the ER is carefully monitored by an ER quality control mechanism that allows only correctly folded proteins to be transported to their final destination, and misfolded or unassembled proteins to be retained in the ER and ...
Jun, Hoseki +2 more
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A luminal flavoprotein in endoplasmic reticulum-associated degradation [PDF]
Proceedings of the National Academy of Sciences, 2009 The quality control system of the endoplasmic reticulum (ER) discriminates between native and nonnative proteins. The latter are degraded by the ER-associated degradation (ERAD) pathway. Whereas many cytosolic and membrane components of this system are known, only few luminal players have been identified.
Riemer, Jan +5 more
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Unraveling the roles of endoplasmic reticulum-associated degradation in metabolic disorders
Frontiers in Endocrinology, 2023 Misfolded proteins retained in the endoplasmic reticulum cause many human diseases. ER-associated degradation (ERAD) is one of the protein quality and quantity control system located at ER, which is responsible for translocating the misfolded proteins or
Hui Luo +7 more
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β-cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency. [PDF]
, 2010 ObjectiveThe islet in type 2 diabetes is characterized by β-cell apoptosis, β-cell endoplasmic reticulum stress, and islet amyloid deposits derived from islet amyloid polypeptide (IAPP).
Butler, Alexandra E +7 more
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Correlation Between Decrease in Protein Levels of Ubiquitin Ligase HRD1 and Amyloid-β Production
Journal of Pharmacological Sciences, 2010 Endoplasmic reticulum–associated degradation (ERAD) is a quality control mechanism in which unfolded proteins are retro-translocated to the cytosol for degradation. Our recent study showed that suppression of expression of ubiquitin ligase HRD1, which is
Ryo Saito +3 more
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Hepatic cytochromes P450: structural degrons and barcodes, posttranslational modifications and cellular adapters in the ERAD-endgame. [PDF]
, 2016 The endoplasmic reticulum (ER)-anchored hepatic cytochromes P450 (P450s) are enzymes that metabolize endo- and xenobiotics i.e. drugs, carcinogens, toxins, natural and chemical products.
Correia, Maria Almira +4 more
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IRE1 phosphatase PP2Ce regulates adaptive ER stress response in the postpartum mammary gland. [PDF]
, 2013 We recently reported that the PPM1l gene encodes an endoplasmic reticulum (ER) membrane targeted protein phosphatase (named PP2Ce) with highly specific activity towards Inositol-requiring protein-1 (IRE1) and regulates the functional outcome of ER stress.
Lane, Timothy F +6 more
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Protein accumulation in the endoplasmic reticulum as a non-equilibrium phase transition [PDF]
, 2014 Several neurological disorders are associated with the aggregation of aberrant proteins, often localized in intracellular organelles such as the endoplasmic reticulum.
Budrikis, Z. +3 more
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The endoplasmic reticulum in plant immunity and cell death [PDF]
, 2012 The endoplasmic reticulum (ER) is a highly dynamic organelle in eukaryotic cells and a major production site of proteins destined for vacuoles, the plasma membrane, or apoplast in plants.
Eichmann, Ruth, Schäfer, P. (Patrick)
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HRDGene Dependence of Endoplasmic Reticulum-associated Degradation [PDF]
Molecular Biology of the Cell, 2000 Work from several laboratories has indicated that many different proteins are subject to endoplasmic reticulum (ER) degradation by a common ER-associated machinery. This machinery includes ER membrane proteins Hrd1p/Der3p and Hrd3p and the ER-associated ubiquitin-conjugating enzymes Ubc7p and Ubc6p.
S, Wilhovsky, R, Gardner, R, Hampton
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