${eta}$-catenin, which plays a critical role in both the cytoskeleton and in transcriptional regulation in variousadherent cell types, undergoes degradation during adherent cell apoptosis. Although ${eta}$-catenin has been reported to be present in Jurkat T-acute lymphoblastic leukemia cells, the regulation of ${eta}$-catenin in hematologic malignancies have not been examined. The data presented here demonstrate that treatment of the T cell leukemia Jurkat iwht the apoptosis inducer anti-Fas induced proteolytic cleavage of ${eta}$-catenin. ${eta}$-catenin was cleaved at both the N- and C-terminus after anti-Fas treatment. Cleavage of intact ${eta}$-catenin was completely inhibited by caspase selective protease inhibitors. These data demonstrate that ${eta}$ -catenin proteolysis is triggered by the cross-linking of the Fas receptor on Jurkat cells and subsequent activation of caspase protease. There was a clear accumulatio of the large proteolytic fragment in Jurkat cells treated with lactacystin of ALLM. These are potent inhibitors of proteasome and calpain. these results suggest that both the proteasome and clapain may recognize the large ${eta}$-catenin fragment as a substrate fot further degradation and that these pathewasy may act downstream of scapase in response to Fas receptor activation. Therefore, we suggest that ${eta}$-catenin may play a role in promoting Jurkat survival.