Influence of Monovalent and Divalent Ions in the Conformational Change of Caspase-Cleaved Par-4 (cl-Par-4) Tumor Suppressor Protein

Autor: Raut, Krishna K.
Rok vydání: 2021
DOI: 10.25883/54ms-q407
Popis: Prostate apoptosis response-4 (Par-4) is a pro-apoptotic tumor suppressor protein. We have shown that this 38 kDa full-length Par-4 (Fl-Par-4) protein is predominantly intrinsically disordered in vitro. In vivo, Par-4 is cleaved by caspase-3 at Asp-131 to generate a 24 kDa functionally active cleaved Par-4 (cl-Par-4) fragment. The cl-Par-4 protein inhibits the NF-κB-mediated cell survival pathway and causes selective apoptosis in various tumor cells. Our laboratory is interested in how the disorder-order balance within Fl-Par-4 and cl-Par-4 may be related to the balance between cell survival and cell death.
Databáze: OpenAIRE