Glutaredoxin: Role in Reversible Protein S-Glutathionylation and Regulation of Redox Signal Transduction and Protein Translocation

摘要: Reversible posttranslational modifications on specific amino acid residues can efficiently regulate protein functions. O-Phosphorylation is the prototype and analogue to rapidly emerging mechanism of regulation known as S-glutathionylation. The latter being recognized a potentially widespread form modulation activities redox-sensitive thiol proteins, especially those involved in signal transduction pathways translocation. abundance reduced glutathione cells ready conversion sulfenic acids S-nitroso derivatives S-glutathione mixed disulfides support notion that reversible S-glutathionylation likely be preponderant mode redox transduction. glutaredoxin enzyme has served focal point important tool for evolution this regulatory because its characterization efficient catalyst protein-SSG de-glutathionylation (akin phosphatases). Identification mechanisms enzyme(s) ...