Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductase*

HIGHLIGHTS

• who: Anton A. Turanov from the Anton ATuranov, Dan Su, and Vadim N. Gladyshev, From the Department of Biochemistry, University of Nebraska, Lincoln, Nebraska, Thioredoxin reductase (TR) and thioredoxin (Trx) define a major cellular redox system that maintains cysteine residues in numerous proteins in the reduced state. Both cytosolic (, and Trx1) and mitochondrial (, and Trx2) enzymes are essential in mammals, but the function of the mitochondrial system is less understood. In this study, we characterized subcellular localization of three , forms that are generated by alternative first exon splicing and that differ in their, terminal sequences. Only one . . .
  

   

  

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