Les deux visages de p63, Janus de la famille p53

Fromentel, Claude Caron de; Aberdam, Édith; Aberdam, Daniel

doi:10.1051/medsci/2012284015

Cited by 3 publications

(3 citation statements)

References 42 publications

(51 reference statements)

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“…De plus, de nombreuses fonctions non transcriptionnelles de p53 ont été décrites et certaines sont probablement impliquées dans le triumvirat [9]. Enfin, il existe deux gènes apparentés à p53, p73 et p63 [55] (➜), dont les rôles se superposent en partie à ceux de p53. Ces trois gènes codent pour de multiples isoformes présentant des fonctions différentes voire opposées [4,10].…”

Section: Le Triumviratunclassified

Protéger et sévir : p53, métabolisme et suppression tumorale

Albagli

2015

Med Sci (Paris)

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Section: Le Triumviratunclassified

Protéger et sévir : p53, métabolisme et suppression tumorale

Albagli

2015

Med Sci (Paris)

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“…p53 is a multifunctional protein that can be activated by a variety of stress signals. p53 can regulate several cellular pathways that determines cell fate, such as cell cycle, differentiation, senescence, and apoptosis (2,17,24). p53 as a tumor suppressor in very early studies has been shown to play a role in various physiological cellular processes (21).…”

Section: Introductionmentioning

confidence: 99%

Orf Virus VIR Antagonizes p53-Mediated Antiviral Effects to Facilitate Viral Replication

et al. 2020

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As a zoonotic disease, ovine contagious pustular dermatitis (Orf) is a serious threat to sheep as well as humans. Orf virus (ORFV) interferon resistance protein (VIR) is the principal virulence protein that encodes a dsRNAbinding protein to inhibit host antiviral response. p53 is one of the key proteins of the host antiviral innate immunity. It not only enhances type I interferon secretion but also induces apoptosis in infected cells, and plays a crucial role in the immune response against various viral infections. However, it remains to be elucidated what role p53 plays in ORFV replication and whether ORFV's own protein VIR regulates p53 expression to promote self-replication. In this study, we showed that p53 has an antiviral effect on ORFV and can inhibit ORFV replication. In addition, ORFV nonstructural protein VIR interacts with p53 and degrades p53, which inhibits p53-mediated positive regulation of downstream antiviral genes. This study provides new insight into the immune evasion mediated by ORFV and identifies VIR as an antagonistic factor for ORFV to evade the antiviral response.

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“…The X-linked inhibitor of apoptosis protein (XIAP) is a member of the IAP family and a potent inhibitor of apoptosis [ 1 , 2 ]. It has been reported that XIAP is upregulated in acute and chronic leukemia [ 3 , 4 ], prostate cancer [ 5 ], breast cancer [ 6 – 8 ], and many other cancers [ 9 – 11 ], thus indicating an association between XIAP overexpression and cancer development [ 12 , 13 ].…”

Section: Introductionmentioning

confidence: 99%

XIAP RING domain mediates miR-4295 expression and subsequently inhibiting p63α protein translation and promoting transformation of bladder epithelial cells

Jin

Guo

et al. 2016

Oncotarget

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The X-linked inhibitor of apoptosis protein (XIAP) contains three N-terminal BIR domains that mediate anti-apoptosis and one C-terminal RING finger domain whose function(s) are not fully defined. Here we show that the RING domain of XIAP strongly inhibits the expression of p63α, a known tumor suppressor. XIAP knockdown in urothelial cells or RING deletion in knockin mice markedly upregulates p63α expression. This RING-mediated p63α downregulation is critical for the malignant transformation of normal urothelial cells following EGF treatment. We further show that the RING domain promotes Sp1-mediated transcription of miR-4295 which targets the 3′UTR of p63α mRNA and consequently inhibits p63α translation. Our results reveal a previously unknown function of the RING of XIAP in promoting miR-4295 transcription, thereby reducing p63α translation and enhancing urothelial transformation. Our data offer novel insights into the multifunctional effects of the XIAP RING domain on urothelial tumorigenesis and the potential for targeting this frequently overexpressed protein as a therapeutic alternative.

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Les deux visages de p63, Janus de la famille p53

Cited by 3 publications

References 42 publications

Protéger et sévir : p53, métabolisme et suppression tumorale

Protéger et sévir : p53, métabolisme et suppression tumorale

Orf Virus VIR Antagonizes p53-Mediated Antiviral Effects to Facilitate Viral Replication

XIAP RING domain mediates miR-4295 expression and subsequently inhibiting p63α protein translation and promoting transformation of bladder epithelial cells

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