Proteolytic Cleavage of Human p53 by Calpain: a Potential Regulator of Protein Stability

• DOI: 10.1128/mcb.17.1.460
• Publication Date: 2015-10-09T22:05:59Z
• Authors: Michael H. G. Kub...; Karen H. Vousden
• Keywords: Proteolysis; Cleavage (geology); Protein Degradation

The p53 tumor suppressor protein is activated in cells response to DNA damage and prevents the replication of sustaining genetic by inducing a cell cycle arrest or apoptosis. Activation accompanied stabilization protein, resulting accumulation high levels within cell. normally degraded through proteasome following ubiquitination, although mechanisms which regulate this proteolysis normal how becomes stabilized are not well understood. We show here that can also be substrate for cleavage calcium-activated neutral protease, calpain, preferential site calpain exists N terminus protein. Treatment expressing wild-type with an inhibitor resulted By contrast, vitro vivo degradation mediated human papillomavirus E6 was unaffected inhibitor, indicating did result from inhibition proteasome. These results suggest plays role regulating stability.