Sestrins (SESN1, SESN2 and likely SESN3) bind overoxidized P...

created [InstanceEdit:5631905] Orlic-Milacic, Marija, 2014-10-27
dbId 5631906
displayName Sestrins (SESN1, SESN2 and likely SESN3) bind overoxidized P...
modified [InstanceEdit:8856610] Orlic-Milacic, Marija, 2016-02-11
schemaClass Summation
text Sestrins (SESN1, SESN2 and likely SESN3) bind overoxidized PRDX1, in which the catalytic cysteine C52 has been converted to cysteine-sulfinic acid. Among all peroxiredoxins, PRDX1 is the most abundant member of the PRDX family. The major function is to protect cells against reactive oxygen species (ROS), thus impacting on cell proliferation and survival (Gong et al. 2015). While several reports state that sestrins reduce overoxidized PRDX1 to the catalytically active homodimer (Budanov et al. 2004, Papadia et al. 2008, Essler et al. 2009), there are conflicting reports claiming that sestrins do not possess cysteine sulfinyl reductase activity (Woo et al. 2009).
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