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

Sayan, AE, Sayan, BS ORCID: https://orcid.org/0000-0003-2305-1970, Gogvadze, V, Dinsdale, G, Nyman, U, Hansen, TM, Zhivotovsky, B, Cohen, GM, Knight, RA and Melino, G 2008, 'p73 and caspase-cleaved p73 fragments localize to mitochondria and augment TRAIL-induced apoptosis' , Oncogene, 27 , pp. 4363-4372.

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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 transcription-independent 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.

Item Type:	Article
Schools:	Schools > School of Environment and Life Sciences
Journal or Publication Title:	Oncogene
Publisher:	Springer Nature
ISSN:	0950-9232
Depositing User:	BS Sayan
Date Deposited:	06 Feb 2023 15:48
Last Modified:	06 Feb 2023 15:48
URI:	https://usir.salford.ac.uk/id/eprint/66348

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