ERO1: A protein disulfide oxidase and H2O2 producer

Zito, Ester

doi:10.1016/j.freeradbiomed.2015.01.011

Cited by 126 publications

(112 citation statements)

References 51 publications

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“…It exists as a collection of oxidized and reduced forms and covalently binds PDI, which catalyzes disulfide formation in newly synthesized proteins entering the mammalian ER [22]. A dynamic equilibrium between Ero1L and glutathione disulfide-mediated oxidation of PDI plays a critical role in ER redox homeostasis and the regulation of Ero1L activity is critical to keep redox homeostasis and proper ER folding activity [23].…”

Section: Discussionmentioning

confidence: 99%

FBXO6-Mediated Ubiquitination and Degradation of Ero1L Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis

Chen

Duan

Luo

et al. 2016

Cell Physiol Biochem

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Background/Aims: FBXO6 is the substrate recognition component of a Skp1-Cullin1-F-box protein (SCF) ubiquitin E3 ligase complex, recognizing the chitobiose in unfolded N-glycoprotein to target glycoproteins for polyubiquitination and degradation. Although how FBXO6 recognizes glycoprotein has been fully investigated, the ubiquitination substrates of FBXO6 remain largely unknown. Previously, we have systematically identified the glycoproteins that interact with FBXO6 in an N-glycan dependent manner by LC/MS spectrum and confirmed the interaction between FBXO6 and glycosylated Ero1L, a protein disulfide oxidase in endoplasmic reticulum (ER). Methods: The relationship between endogenous Ero1L and exogenous Flag-FBXO6 were determined by Western blot. In vivo ubiquitination assay was used to detect the direct effect of FBXO6 in the regulation of Ero1L. Both CCK8 and FACS assays were used to determine the apoptosis ratio of cells after treatments. Results: Ero1L is a ubiquitination substrate of FBXO6. FBXO6 mediates the degradation of Ero1L through a ubiquitylation-dependent pathway. Overexpression of FBXO6 increased the polyubiquitination and decreased the stability of Ero1L, whereas inhibition of FBXO6 prolonged the half-life of Ero1L. Functionally, we show that FBXO6 inhibits ER stress-induced apoptosis by modulating the protein level of Ero1L. Conclusion: Collectively, our results demonstrate FBXO6 as a functional E3 ubiquitin ligase for Ero1L that plays a critical role in inhibiting ER stress-induced apoptosis.

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Section: Discussionmentioning

confidence: 99%

FBXO6-Mediated Ubiquitination and Degradation of Ero1L Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis

Chen

Duan

Luo

et al. 2016

Cell Physiol Biochem

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“…Thus, the coordinated function of ERO1 and PRDX4 during oxidative protein folding in the ER constitutes a safe and efficient system in mammalian cells. The mechanism of this system is discussed in detail in this issue of the journal [17,43]; hence, we need go no further.…”

Section: Roles Of Prdx4 In the Ermentioning

confidence: 99%

“…Compared with other mammalian PRDX members, the reports of the localization and roles of PRDX4 are conflicting [13][14][15][16]. Recently, an understanding of the roles of PRDX4 has markedly advanced, particularly concerning the sulfoxidase function in the endoplasmic reticulum (ER) [17]. Because PRDX4 is also present extracellularly, we are proposing a hypothetical function acknowledging that defining its function remains a future challenge.…”

Section: Introductionmentioning

confidence: 99%

Physiological and pathological views of peroxiredoxin 4

Fujii

Ikeda

Kurahashi

et al. 2015

Free Radical Biology and Medicine

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“…The ER provides the critical function of folding newly synthesized proteins and then sorting them for various cellular addresses (Chen et al 2013). ER protein folding utilizes specialized chaperones (protein disulfide isomerases and Ero1) and an oxidative environment (Pollard et al 1998) resulting in conversion of oxygen to H 2 O 2 (Zito 2015). Defects in protein folding trigger the well-studied unfolded protein response (UPR) that induces ERO1 transcription.…”

Section: Internal Sources Of Rosmentioning

confidence: 99%

Programmed Cell Death Initiation and Execution in Budding Yeast

Strich

2015

Genetics

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Apoptosis or programmed cell death (PCD) was initially described in metazoans as a genetically controlled process leading to intracellular breakdown and engulfment by a neighboring cell . This process was distinguished from other forms of cell death like necrosis by maintenance of plasma membrane integrity prior to engulfment and the well-defined genetic system controlling this process. Apoptosis was originally described as a mechanism to reshape tissues during development. Given this context, the assumption was made that this process would not be found in simpler eukaryotes such as budding yeast. Although basic components of the apoptotic pathway were identified in yeast, initial observations suggested that it was devoid of prosurvival and prodeath regulatory proteins identified in mammalian cells. However, as apoptosis became extensively linked to the elimination of damaged cells, key PCD regulatory proteins were identified in yeast that play similar roles in mammals. This review highlights recent discoveries that have permitted information regarding PCD regulation in yeast to now inform experiments in animals.

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ERO1: A protein disulfide oxidase and H2O2 producer

Cited by 126 publications

References 51 publications

FBXO6-Mediated Ubiquitination and Degradation of Ero1L Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis

FBXO6-Mediated Ubiquitination and Degradation of Ero1L Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis

Physiological and pathological views of peroxiredoxin 4

Programmed Cell Death Initiation and Execution in Budding Yeast

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