4.6 Review

Selenoprotein S: A versatile disordered protein

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Effects of Selenoprotein S Knockdown on Endoplasmic Reticulum Stress in ATDC5 Cells and Gene Expression Profiles in Hypertrophic Chondrocytes

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Summary: SelS is a selenium-sensitive protein involved in various biological processes in chondrocytes, including ER stress. Knocking down SelS results in abnormal expression of adhesion molecules and matrix homeostasis in hypertrophic chondrocytes.

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An Integrated In Silico, In Vitro and Tumor Tissues Study Identified Selenoprotein S (SELENOS) and Valosin-Containing Protein (VCP/p97) as Novel Potential Associated Prognostic Biomarkers in Triple Negative Breast Cancer

Susan Costantini et al.

Summary: In this study, the expression profiles of twenty-five human selenoproteins in triple negative breast cancer (TNBC) were analyzed. It was found that five selenoproteins were specifically dysregulated in TNBC. Additionally, selenoprotein S and its interacting protein valosin-containing protein (VCP/p97) were identified as mechanistically related proteins whose coordinated over-expression was associated with poor prognosis in TNBC.

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HSF1-SELENOS pathway mediated dietary inorganic Se-induced lipogenesis via the up-regulation of PPARγ expression in yellow catfish

Dian-Guang Zhang et al.

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Hepatic deficiency of selenoprotein S exacerbates hepatic steatosis and insulin resistance

Lu Qiao et al.

Summary: This study reveals the important regulatory role of SelS in NAFLD and T2DM. SelS deficiency in the liver leads to increased ER stress, increased fatty acid uptake, and decreased fatty acid oxidation, resulting in hepatic steatosis. SelS deficiency also disrupts insulin signaling and impairs glucose metabolism. Additionally, activation of hepatic protein kinase Ce is involved in the negative regulation of SelS. The inhibitory effects of SelS on hepatic steatosis and insulin resistance are confirmed in vitro experiments.

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Regulation of A-to-I RNA editing and stop codon recoding to control selenoprotein expression during skeletal myogenesis

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Quantifying Turnover Dynamics of Selenoproteome by Isotopic Perturbation

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Selenoprotein S regulates tumorigenesis of clear cell renal cell carcinoma through AKT/ GSK3β/NF-κB signaling pathway

Huajie Mao et al.

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The selenoprotein P 3′ untranslated region is an RNA binding protein platform that fine tunes selenocysteine incorporation

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Summary: Selenoproteins contain selenocysteine and their mRNA 3'UTRs are not conserved, while the 3'UTR of a given selenoprotein is often conserved across species. We identified PTBP1 as a RNA binding protein that interacts specifically with the sequence between two SECIS elements. Deletion of regions surrounding the first SECIS element affects SELENOP mRNA and protein levels in response to selenium concentrations.

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Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon

Tarek Hilal et al.

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Logesvaran Krshnan et al.

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The Associations of Selenoprotein Genetic Variants with the Risks of Colorectal Adenoma and Colorectal Cancer: Case-Control Studies in Irish and Czech Populations

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Selenoprotein K Is Essential for the Migration and Phagocytosis of Immature Dendritic Cells

Huan Xia et al.

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Selenoprotein S regulates tumorigenesis of clear cell renal cell carcinoma through AKT/ GSK3 beta/NF-Kappa B signaling pathway

Huajie Mao et al.

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SAA1 is transcriptionally activated by STAT3 and accelerates renal interstitial fibrosis by inducing endoplasmic reticulum stress

Fan Zhang et al.

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Selenoprotein S attenuates high glucose and/or ox-LDL-induced endothelium injury by regulating Akt/mTOR signaling and autophagy

Zinan Wang et al.

Summary: The study found that high glucose and high oxidized low-density lipoprotein can reduce the viability of human aortic endothelial cells and increase SelS expression. SelS overexpression can reduce endothelial injury and autophagy while activating the Akt/mTOR signaling. This suggests that SelS may be a potential target for preventing and treating diabetic vascular complications.

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY (2021)

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Pathogenic Variants in Selenoproteins and Selenocysteine Biosynthesis Machinery

Didac Santesmasses et al.

Summary: Selenium is incorporated into selenoproteins as the 21st amino acid selenocysteine (Sec). There are 25 selenoproteins encoded in the human genome, and their synthesis requires a dedicated machinery. Most selenoproteins are oxidoreductases with important functions in human health. Deficiencies in selenoproteins can lead to various disorders, with mutations in selenoprotein genes or Sec machinery genes being common causes.

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Qianru Chi et al.

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Yijun Wang et al.

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