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Antioxid Redox Signal. 2015 Oct 1;23(10):795-813. doi: 10.1089/ars.2015.6388. Epub 2015 Jul 13.

Membrane-bound selenoproteins.

Author information

1
Department of Chemistry and Biochemistry, University of Delaware , Newark, Delaware.

Abstract

SIGNIFICANCE:

Selenoproteins employ selenium to supplement the chemistry available through the common 20 amino acids. These powerful enzymes are affiliated with redox biology, often in connection with the detection, management, and signaling of oxidative stress. Among them, membrane-bound selenoproteins play prominent roles in signaling pathways, Ca(2+) regulation, membrane complexes integrity, and biosynthesis of lipophilic molecules.

RECENT ADVANCES:

The number of selenoproteins whose physiological roles, protein partners, expression, evolution, and biosynthesis are characterized is steadily increasing, thus offering a more nuanced view of this specialized family. This review focuses on human membrane selenoproteins, particularly the five least characterized ones: selenoproteins I, K, N, S, and T.

CRITICAL ISSUES:

Membrane-bound selenoproteins are the least understood, as it is challenging to provide the membrane-like environment required for their biochemical and biophysical characterization. Hence, their studies rely mostly on biological rather than structural and biochemical assays. Another aspect that has not received much attention is the particular role that their membrane association plays in their physiological function.

FUTURE DIRECTIONS:

Findings cited in this review show that it is possible to infer the structure and the membrane-binding mode of these lesser-studied selenoproteins and design experiments to examine the role of the rare amino acid selenocysteine.

PMID:
26168272
DOI:
10.1089/ars.2015.6388
[Indexed for MEDLINE]

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