Please use this identifier to cite or link to this item:
|Title:||p73 and caspase-cleaved p73 fragments localize to mitochondria and augment TRAIL-induced apoptosis|
|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|
|Description:||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.2008.64|
Metadata only entry
|Appears in Collections:||Published Articles, MRC Toxicology Unit|
Files in This Item:
There are no files associated with this item.
Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.