Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress.
Protein S-glutathiolation, the reversible covalent addition of glutathione to cysteine residues on target proteins, is emerging as a candidate mechanism by which both changes in the intracellular redox state and the generation of reactive oxygen and nitrogen species may be transduced into a functional response. This review will provide an introduction to the concepts of oxidative and nitrosative stress and outline the molecular mechanisms of protein regulation by oxidative and nitrosative thiol-group modifications. Special attention will be paid to recently published work supporting a role for S-glutathiolation in stress signalling pathways and in the adaptive cellular response to oxidative and nitrosative stress. Finally, novel insights into the molecular mechanisms of S-glutathiolation as well as methodological problems related to the interpretation of the biological relevance of this post-translational protein modification will be discussed.
Department of Estructura y Función de Proteínas, Centro de Investigaciones Biológicas, Instituto Reina Sofía de Investigaciones Nefrológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain. pklatt@cnb.uam.es
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D000818:Animals; D005978:Glutathione / Q000378:metabolism*; D006801:Humans; D009569:Nitric Oxide / Q000502:physiology; D015538:Nitrosation; D018384:Oxidative Stress; D011506:Proteins / Q000378:metabolism*; D015398:Signal Transduction
D011506:Proteins; D009569:Nitric Oxide; D005978:Glutathione