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p73 and caspase-cleaved p73 fragments localize to mitochondria and augment TRAIL-induced apoptosis

By A.E. Sayan, B.S. Sayan, V. Gogvadze, D. Dinsdale, U. Nyman, T.M. Hansen, B. Zhivotovsky, G.M. Cohen, R.A. Knight and G. Melino

Abstract

This paper was published as Oncogene, 2008, 27 (31), pp. 4363-4372. It is available from http://www.nature.com/onc/journal/v27/n31/index.html. Doi: 10.1038/onc.2008.64Metadata only entryThe p73 protein, a member of the p53 family, has both\ud developmental and tumorigenic functions. Here we show\ud that p73 is cleaved by caspase-3 and -8 both in vitro and in\ud vivo during apoptosis elicited by DNA-damaging drugs\ud and tumor necrosis factor-related apoptosis-inducing\ud ligand (TRAIL) receptor ligation. TAp73 and some of\ud its cleavage products are localized to mitochondria.\ud siRNA-mediated downregulation of p73 expression induced\ud a small but significant change in the susceptibility of\ud HCT116 cells to TRAIL-induced apoptosis. A transcription-\ud deficient mutant of TAp73 enhanced TRAIL-induced\ud apoptosis suggesting that p73 protein has transcriptionindependent\ud functions during death receptor-mediated\ud apoptosis. Additionally, recombinant p73 protein induced\ud cytochrome c release from isolated mitochondria providing\ud evidence that nonnuclear p73 may have additional\ud functions in the progression of apoptosi

Publisher: Nature Publishing Group
Year: 2008
DOI identifier: 10.1038/onc.2008.64
OAI identifier: oai:lra.le.ac.uk:2381/9123
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