Erv2 and Quiescin Sulfhydryl Oxidases: Erv-Domain Enzymes Associated with the Secretory Pathway

Sevier, Carolyn S.

doi:10.1089/ars.2011.4450

Cited by 17 publications

(17 citation statements)

References 59 publications

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“…Quiescin-Sulfhydryl Oxidase (QSOX) proteins are produced in the ER and catalyze disulfide formation, thereby generating peroxide, but their contributions to ER protein folding in vivo are unknown (Kodali and Thorpe, 2010; Sevier, 2012). Strikingly, ero-1 RNAi failed to generate ROS and activate p38 when C. elegans QSOX genes were knocked down (Figure S4G and S4H).…”

Section: Resultsmentioning

confidence: 99%

Cysteine Sulfenylation Directs IRE-1 to Activate the SKN-1/Nrf2 Antioxidant Response

et al. 2016

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SUMMARY Emerging evidence suggests that many proteins may be regulated through cysteine modification, but the extent and functions of this signaling remain largely unclear. The endoplasmic reticulum (ER) transmembrane protein IRE-1 maintains ER homeostasis by initiating the unfolded protein response (UPRER). Here we show in C. elegans and mammalian cells that IRE-1 has a distinct redox-regulated function in cytoplasmic homeostasis. Reactive oxygen species (ROS) that are generated at the ER or by mitochondria sulfenylate a cysteine within the IRE-1 kinase activation loop. This inhibits the IRE-1-mediated UPRER, and initiates the p38/SKN-1(Nrf2) antioxidant response, thereby increasing stress resistance and lifespan. Many AGC-family kinases (AKT, p70S6K, PKC, ROCK1) seem to be regulated similarly. The data reveal that IRE-1 has an ancient function as a cytoplasmic sentinel that activates p38 and SKN-1(Nrf2), and indicate that cysteine modifications induced by ROS signals can direct proteins to adopt unexpected functions, and may coordinate many cellular processes.

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Section: Resultsmentioning

confidence: 99%

Cysteine Sulfenylation Directs IRE-1 to Activate the SKN-1/Nrf2 Antioxidant Response

et al. 2016

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“…QSOX1 encodes a protein belonging to the family of enzymes that catalyze disulfide bond formation and are important for cell growth [15] and was 3x higher than lung and almost 9x higher than adipose, breast, heart, kidney liver and smooth muscle (Table 2). Similar results were confirmed for QSOX1 expression using qRT-PCR, with the exception of placenta vs. lung expression (Figure 2A).…”

Section: Resultsmentioning

confidence: 99%

A comprehensive analysis of the human placenta transcriptome

et al. 2014

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As the conduit for nutrients and growth signals, the placenta is critical to establishing an environment sufficient for fetal growth and development. To better understand the mechanisms regulating placental development and gene expression, we characterized the transcriptome of term placenta from 20 healthy women with uncomplicated pregnancies using RNA-seq. To identify genes that were highly expressed and unique to the placenta we compared placental RNA-seq data to data from 7 other tissues (adipose, breast, hear, kidney, liver, lung, and smooth muscle) and identified several genes novel to placental biology (QSOX1, DLG5, and SEMA7A). Semi-quantitative RT-PCR confirmed the RNA-seq results and immunohistochemistry indicated these proteins were highly expressed in the placental syncytium. Additionally, we mined our RNA-seq data to map the relative expression of key developmental gene families (Fox, Sox, Gata, Tead, and Wnt) within the placenta. We identified FOXO4, GATA3, and WNT7A to be amongst the highest expressed members of these families. Overall, these findings provide a new reference for understanding of placental transcriptome and can aid in the identification of novel pathways regulating placenta physiology that may be dysregulated in placental disease.

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“…Electrons may be shuttled from Ero1 or the yeast-specific sulfhydryl oxidase Erv2, which is a homologue of Erv1 (Sevier, 2012). An open question is the mechanism by which fumarate may be transported into the ER, because a specific transporter has not been identified.…”

Section: Discussionmentioning

confidence: 99%

“…PDI is then maintained in an oxidized state by the sulfhydryl oxidase Ero1, and electrons are subsequently donated to O 2 , generating hydrogen peroxide (Tu et al , 2000). Yeasts also have a second sulfhydryl oxidase Erv2 that has an auxiliary role in oxidizing ER proteins (Sevier, 2012). In contrast, studies indicate that mammals may use vitamin K epoxide reductase, quiescin sulfhydryl oxidase, and/or peroxiredoxin IV as Ero1 alternatives (Mairet-Coello et al , 2004; Wajih et al , 2007; Zito et al , 2010).…”

Section: Introductionmentioning

confidence: 99%

Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space

Neal

Dabir

Wijaya

et al. 2017

MBoC

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Erv2 and Quiescin Sulfhydryl Oxidases: Erv-Domain Enzymes Associated with the Secretory Pathway

Cited by 17 publications

References 59 publications

Cysteine Sulfenylation Directs IRE-1 to Activate the SKN-1/Nrf2 Antioxidant Response

Cysteine Sulfenylation Directs IRE-1 to Activate the SKN-1/Nrf2 Antioxidant Response

A comprehensive analysis of the human placenta transcriptome

Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space

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