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. 2020 Apr 15;7:60. doi: 10.3389/fmolb.2020.00060

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Copyright © 2020 Hoter, Rizk and Naim.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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A schematic representation summarizing the roles of HSP60 in regulating tumor cell apoptosis. Suppression of apoptosis by HSP60 is associated with increased levels of anti-apoptotic proteins like Bcl-2, Bcl-xL, and survivin. These molecules counteract the release of cytochrome c from mitochondria. Selectively in tumor cells, HSP60 forms a multichaperone complex with Cyclophilin D (Cyp D) and other chaperones including HSP90 and tumor necrosis factor receptor-associated protein 1 (TNFRP1) to maintain the mitochondrial permeability transition. Oncogenic HSP60 interacts with p53 in tumor cells and suppresses its action. HSP60 also controls the progression of apoptosis via regulating the mitochondrial release of smac/diablo and controlling the function of inhibitor of apoptosis (IAP) family proteins that inhibit caspases.