Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/14302
ชื่อเรื่อง: Apoptin induces apoptosis by changing the equilibrium between the stability of TAp73 and DNp73 isoforms through ubiquitin ligase PIR2
ผู้แต่ง: Taebunpakul P.
Sayan B.S.
Flinterman M.
Klanrit P.
Gäken J.
Odell E.W.
Melino G.
Tavassoli M.
Keywords: apoptin
protein p53
protein p73
PUMA protein
small interfering RNA
ubiquitin protein ligase
ubiquitin protein ligase E3
ubiquitin protein ligase PIR2
unclassified drug
apoptosis
article
controlled study
cytotoxicity
Gyrovirus
human
human cell
priority journal
protein expression
protein stability
RING finger motif
Apoptosis
Apoptosis Regulatory Proteins
Capsid Proteins
Cell Line, Tumor
DNA-Binding Proteins
G2 Phase Cell Cycle Checkpoints
Half-Life
Humans
Nuclear Proteins
Poly(ADP-ribose) Polymerases
Protein Isoforms
Protein Processing, Post-Translational
Protein Stability
Proteolysis
Proto-Oncogene Proteins
Tumor Suppressor Protein p53
Tumor Suppressor Proteins
Ubiquitin-Protein Ligases
Ubiquitination
Chicken anemia virus
วันที่เผยแพร่: 2012
บทคัดย่อ: Apoptin, a protein derived from the chicken anaemia virus, induces cell death in various cancer cells but shows little or no cytotoxicity in normal cells. The mechanism of apoptin-induced cell death is currently unknown but it appears to induce apoptosis independent of p53 status. Here we show that p73, a p53 family member, is important in apoptin-induced apoptosis. In p53 deficient and/or mutated cells, apoptin induced the expression of TAp73 leading to the induction of apoptosis. Knockdown of p73 using siRNA resulted in a significant reduction in apoptin-induced cytotoxicity. The p53 and p73 pro-apoptotic target PUMA plays an important role in apoptin-induced cell death as knockdown of PUMA significantly reduced cell sensitivity to apoptin. Importantly, apoptin expression resulted in a marked increase in TAp73 protein stability. Investigation into the mechanisms of TAp73 stability showed that apoptin induced the expression of the ring finger domain ubiquitin ligase PIR2 which is involved in the degradation of the anti-apoptotic DNp73 isoform. Collectively, our results suggest a novel mechanism of apoptin-induced apoptosis through increased TAp73 stability and induction of PIR2 resulting in the degradation of DNp73 and activation of pro-apoptotic targets such as PUMA causing cancer cell death. © Springer Science+Business Media, LLC 2012.
URI: https://ir.swu.ac.th/jspui/handle/123456789/14302
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84865152602&doi=10.1007%2fs10495-012-0720-7&partnerID=40&md5=be2bce89c119ba8f18998fce65431b00
ISSN: 13608185
Appears in Collections:Scopus 1983-2021

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