Thioredoxin-1 and posttranslational modifications.
Thioredoxin-1 is a 12 kDa protein that consists of a redox regulatory domain containing the active cysteine residues 32 and 35. These cysteines are conserved from bacteria to human. Unlike thioredoxins from lower species, mammalian thioredoxin-1 contains three additional nonactive cysteine residues at positions 62, 69, and 73 (for human thioredoxin-1). Key biological functions of thioredoxin-1 are antioxidative, anti-apoptotic, and pro-proliferative properties. Thioredoxin-1 is regulated by the ability of the thioredoxin reductase to reduce oxidized thioredoxin-1 at cysteines 32 and 35. However, posttranslational modifications of thioredoxin-1, including glutathionylation, thiol-oxidation, and S-nitros(yl)ation, at the nonactive cysteines importantly contribute to the regulation and functions of thioredoxin-1. This review focuses on the posttranslational modifications of the active and nonactive cysteines and their contribution for functional regulation of thioredoxin-1.
Haendeler
Judith
J
Molecular Cardiology, Department of Internal Medicine III, University of Frankfurt, Frankfurt, Germany. j.haendeler@em.uni-frankfurt.de
D000818:Animals; D003545:Cysteine / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism; D006801:Humans; D009569:Nitric Oxide / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D026403:S-Nitrosothiols / Q000737:chemistry / Q000378:metabolism; D013879:Thioredoxins / Q000378:metabolism*
D026403:S-Nitrosothiols; C491203:TXN protein, human; D009569:Nitric Oxide; D013879:Thioredoxins; D005978:Glutathione; D003545:Cysteine