Identification of selenoprotein O substrates using a biotinylated ATP analog

Mukherjee, Meghomukta; Sreelatha, Anju

doi:10.1016/bs.mie.2021.10.001

Cited by 1 publication

(1 citation statement)

References 23 publications

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“…197 Selenoprotein O SEL O Shown to participate in bacterial protein ampylation. 198 Implicated in maintenance of mitochondrial function in response to selenomethionine supplementation in murine AD models. 199 Selenoprotein T SEL T Thioredoxin-like structure with oxidoreductase activity.…”

Section: Selenium Transport and Storagementioning

confidence: 99%

Selenoproteins and the senescence-associated epitranscriptome

Lee

Ojeda-Britez

Ehrbar

et al. 2022

Exp Biol Med (Maywood)

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Selenium is a naturally found trace element, which provides multiple benefits including antioxidant, anticancer, and antiaging, as well as boosting immunity. One unique feature of selenium is its incorporation as selenocysteine, a rare 21st amino acid, into selenoproteins. Twenty-five human selenoproteins have been discovered, and a majority of these serve as crucial antioxidant enzymes for redox homeostasis. Unlike other amino acids, incorporation of selenocysteine requires a distinctive UGA stop codon recoding mechanism. Although many studies correlating selenium, selenoproteins, aging, and senescence have been performed, it has not yet been explored if the upstream events regulating selenoprotein synthesis play a role in senescence-associated pathologies. The epitranscriptomic writer alkylation repair homolog 8 (ALKBH8) is critical for selenoprotein production, and its deficiency can significantly decrease levels of selenoproteins that are essential for reactive oxygen species (ROS) detoxification, and increase oxidative stress, one of the major drivers of cellular senescence. Here, we review the potential role of epitranscriptomic marks that govern selenocysteine utilization in regulating the senescence program.

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Section: Selenium Transport and Storagementioning

confidence: 99%