Selenoprotein T: From Discovery to Functional Studies Using Conditional Knockout Mice

Boukhzar, Loubna; Tanguy, Yannick; Abid, Houssni; Castex, Matthieu; Hamieh, Abdallah; Alsharif, Ifat; Cartier, Dorthe; Prévost, Gaëtan; Falluel‐Morel, Anthony; Lihrmann, Isabelle; Chagraoui, Abdeslam; Anouar, Youssef

doi:10.1007/978-3-319-41283-2_23

Cited by 6 publications

(4 citation statements)

References 42 publications

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“…Thus, by biochemical definition, CH3Hg + is a highly selective irreversible inhibitor of selenoenzymes. In addition to coinciding with observations of increased oxidative damage, inhibition of SELENOT results in increased cellular free calcium and increased catecholamine release (Grumolato et al, 2008;Uezono et al, 2006;Baoukhzar et al, 2016). This could arise through direct binding to the active site Sec of SELENOT or as a result of depletion of biologically available Se resulting it its absence.…”

Section: Silencing Of Selenoenzymes (Sos-2)supporting

confidence: 54%

Mercury's neurotoxicity is characterized by its disruption of selenium biochemistry

Ralston

Raymond

2018

Biochimica et Biophysica Acta (BBA) - General Subjects

144

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Section: Silencing Of Selenoenzymes (Sos-2)supporting

confidence: 54%

Mercury's neurotoxicity is characterized by its disruption of selenium biochemistry

Ralston

Raymond

2018

Biochimica et Biophysica Acta (BBA) - General Subjects

144

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“…SELENOT is a thioredoxin-like enzyme localized to the ER membrane that was initially identified using an algorithm that searched for mRNAs containing a selenocysteine insertion element (SECIS) in the 3’ untranslated region (UTR) [103]. Structurally, SELENOT contains a signal peptide, a thioredoxin-like fold with a Sec residue in the active site, and two hydrophobic stretches (residues 87–102 and 125–143) indicative of transmembrane domains [104]. It is presumed to modulate ER thiol redox balance and recent in vitro studies have shown that it exhibits thioredoxin reductase-like activity [105].…”

Section: Regulation Of Ca2+ Signaling By Er-resident Selenoproteinsmentioning

confidence: 99%

“…This paper determined that SELENOT upregulation was dependent upon increased levels of cAMP and intracellular Ca 2+ flux in response to PACAP. More recent studies investigating the nature of the PACAP-induced signal activating SELENOT gene transcription unveiled a pathway involving protein kinase A, AMP kinase, and peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1-α) that is coupled to mitochondrial biogenesis [104].…”

Section: Regulation Of Ca2+ Signaling By Er-resident Selenoproteinsmentioning

confidence: 99%

Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis

2018

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The human selenoprotein family contains 25 members that share the common feature of containing the amino acid, selenocysteine (Sec). Seven selenoproteins are localized to the endoplasmic reticulum (ER) and exhibit different structural features contributing to a range of cellular functions. Some of these functions are either directly or indirectly related to calcium (Ca) flux or homeostasis. The presence of the unique Sec residue within these proteins allows some to exert oxidoreductase activity, while the function of the Sec in other ER selenoproteins remains unclear. Some functional insight has been achieved by identifying domains within the ER selenoproteins or through the identification of binding partners. For example, selenoproteins K and N (SELENOK AND SELENON) have been characterized through interactions detected with the inositol 1,4,5-triphosphate receptors (IP3Rs) and the SERCA2b pump, respectively. Others have been linked to chaperone functions related to ER stress or Ca homeostasis. This review summarizes the details gathered to date regarding the ER-resident selenoproteins and their effect on Ca regulated pathways and outcomes in cells.

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“…The presence of a hydrophobic transmembrane domain led to the discovery of SELENOT as integrated within the ER membrane. There, it closely resembles thioredoxin reductase activity, as it has been seen to reduce 5,5′-dithio-bis to 5-thio-2-nitrobenzoic acid in the presence of NADPH (Boukhzar et al, 2016).…”

Section: Selenoprotein T (Selenot Selt)mentioning

confidence: 80%

The role of selenoproteins in neurodevelopment and neurological function: Implications in autism spectrum disorder

Behl

Mehta

Pandey

2023

Front. Mol. Neurosci.

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Selenium and selenoproteins play a role in many biological functions, particularly in brain development and function. This review outlines the role of each class of selenoprotein in human brain function. Most selenoproteins play a large antioxidant role within the brain. Autism spectrum disorder (ASD) has been shown to correlate with increased oxidative stress, and the presumption of selenoproteins as key players in ASD etiology are discussed. Further, current literature surrounding selenium in ASD and selenium supplementation studies are reviewed. Finally, perspectives are given for future directions of selenoprotein research in ASD.

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Selenoprotein T: From Discovery to Functional Studies Using Conditional Knockout Mice

Cited by 6 publications

References 42 publications

Mercury's neurotoxicity is characterized by its disruption of selenium biochemistry

Mercury's neurotoxicity is characterized by its disruption of selenium biochemistry

Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis

The role of selenoproteins in neurodevelopment and neurological function: Implications in autism spectrum disorder

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