title: Membrane-bound selenoproteins.
abstract: CONCLUSIONS
  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.
  
  
  BACKGROUND
  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.
  
  
  RESULTS
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Department of Chemistry and Biochemistry, University of Delaware , Newark, Delaware.
authors.forename: Jun
authors.initials: J
authors.lastname: Liu
authors.affiliation: Department of Chemistry and Biochemistry, University of Delaware , Newark, Delaware.
authors.forename: Sharon
authors.initials: S
authors.lastname: Rozovsky
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D017279:Selenocysteine / Q000378:metabolism; D051140:Selenoproteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D051140:Selenoproteins; D017279:Selenocysteine