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Title: p73 and caspase-cleaved p73 fragments localize to mitochondria and augment TRAIL-induced apoptosis
Authors: Sayan, A.E.
Sayan, B.S.
Gogvadze, V.
Dinsdale, D.
Nyman, U.
Hansen, T.M.
Zhivotovsky, B.
Cohen, G.M.
Knight, R.A.
Melino, G.
First Published: 24-Mar-2008
Publisher: Nature Publishing Group
Citation: Oncogene, 2008, 27 (31), pp. 4363-4372.
Abstract: The p73 protein, a member of the p53 family, has both developmental and tumorigenic functions. Here we show that p73 is cleaved by caspase-3 and -8 both in vitro and in vivo during apoptosis elicited by DNA-damaging drugs and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) receptor ligation. TAp73 and some of its cleavage products are localized to mitochondria. siRNA-mediated downregulation of p73 expression induced a small but significant change in the susceptibility of HCT116 cells to TRAIL-induced apoptosis. A transcription- deficient mutant of TAp73 enhanced TRAIL-induced apoptosis suggesting that p73 protein has transcriptionindependent functions during death receptor-mediated apoptosis. Additionally, recombinant p73 protein induced cytochrome c release from isolated mitochondria providing evidence that nonnuclear p73 may have additional functions in the progression of apoptosis
ISSN: 0950-9232
Type: Article
Description: This paper was published as Oncogene, 2008, 27 (31), pp. 4363-4372. It is available from Doi: 10.1038/onc.2008.64
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Appears in Collections:Published Articles, MRC Toxicology Unit

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