An isomerase completes the circuit for a redox switch.

The Journal of Biological Chemistry
Gustavo Salinas

Abstract

The activity of human transglutaminase 2 (TG2), which forms protein cross-links between glutamine and lysine residues, is controlled by an allosteric disulfide bond. However, the mechanism by which this bond is formed, like many systems regulated by oxidative cysteine modifications, was not clear. A new study from Khosla and colleagues shows that TG2 is oxidatively inactivated by the protein disulfide isomerase ERp57, providing the first example of a defined and reversible protein-controlled redox switch and pointing to new strategies to inhibit undesirable TG2 activity in pathological states.

References

Dec 21, 2007·PLoS Biology·Daniel M PinkasChaitan Khosla
Sep 14, 2010·Antioxidants & Redox Signaling·Iman AzimiPhilip J Hogg
Sep 13, 2011·The Journal of Biological Chemistry·Xi JinChaitan Khosla
Feb 14, 2014·Blood·Diego ButeraPhilip J Hogg
Apr 3, 2014·Physiological Reviews·Richard L EckertKapil Mehta
Nov 19, 2014·Proceedings of the National Academy of Sciences of the United States of America·Rasmus IversenLudvig M Sollid
Jan 7, 2018·The Journal of Biological Chemistry·Michael C YiChaitan Khosla

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