Abstract 2163 REDD2 protein abundance is controlled by redox-sensitive proteasomal degradation

degradation assays confirmed that phosphorylated CTNNA3 (5D) was degraded more rapidly than unphosphorylated (5A) or wild-type CTNNA3, highlighting the role of phosphorylation in targeting CTNNA3 for proteasome-mediated degradation.Finally, co-immunoprecipitation experiments revealed that fortilin preferentially binds to unphosphorylated CTNNA3, further supporting its role in protecting CTNNA3 from phosphorylation and subsequent degradation.Moreover, silencing CTNNA3 leads to a significant increase in apoptosis, emphasizing its critical role in maintaining cellular integrity.Our findings highlight the novel role of CTNNA3 as a dualfunction protein-serving as both a structural component of adherens junctions and a key regulator in cell survival pathways.These results provide new insights into fortilin's antiapoptotic mechanisms and suggest that this pathway may be relevant for understanding and addressing diseases associated with CTNNA3 dysfunction.