Bax/Bak activation in the absence of Bid, Bim, Puma, and p53

Zhang, J; Huang, Kai; O’Neill, Katelyn; Pang, Xiaming; Luo, Xu

doi:10.1038/cddis.2016.167

Cited by 56 publications

(46 citation statements)

References 62 publications

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“…On the contrary to the tumour promoting character, integrin b4 has also been linked to cell growth arrest and apoptosis via activating p53 function [55,59,[72][73][74][75][76][77]. Since TAp73 is a well-known inducer of apoptosis, it is reasonable to speculate that the regulation of TAp73 on integrin b4 could influence the apoptosis-related signaling.…”

Section: Resultsmentioning

confidence: 99%

Integrin-β4 is a novel transcriptional target of TAp73

Xie

Vikhreva

Annicchiarico-Petruzzelli

et al. 2018

Cell Cycle

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As a member of p53 family, p73 has attracted intense investigations due to its structural and functional similarities to p53. Among more than ten p73 variants, the transactivation (TA) domain-containing isoform TAp73 is the one that imitates the p53's behavior most. TAp73 induces apoptosis and cell cycle arrest, which endows it the capacity of tumour suppression. Also, it can exert diverse biological influences on cells through activating a complex and context dependent transcriptional programme. The transcriptional activities further broaden its roles in more intricate biological processes. In this article, we report that p73 is a positive regulator of a cell adhesion related gene named integrin β4 (ITGB4). This finding may have implications for the dissection of the biological mechanisms underlining p73 functions.

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Section: Resultsmentioning

confidence: 99%

Integrin-β4 is a novel transcriptional target of TAp73

Xie

Vikhreva

Annicchiarico-Petruzzelli

et al. 2018

Cell Cycle

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“…These observations are consistent with a recent study by O'Neill and colleagues. 32, 33 Their genome editing experiments show that Bax and Bak can initiate oligomerization in the absence of any other Bcl-2 protein, including Bid. Interactions with the OMM are sufficient to Bax and Bak to be activated at the initiation of apoptosis.…”

Section: Discussionmentioning

confidence: 99%

Bcl-2 proteins bid and bax form a network to permeabilize the mitochondria at the onset of apoptosis

2016

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The most critical step in the initiation of apoptosis is the activation of the Bcl-2 family of proteins to oligomerize and permeabilize the outer-mitochondrial membrane (OMM). As this step results in the irreversible release of factors that enhance cellular degradation, it is the point of no return in programmed cell death and would be an ideal therapeutic target. However, the arrangement of the Bcl-2 proteins in the OMM during permeabilization still remains unknown. It is also unclear whether the Bcl-2 protein, Bid, directly participates in the formation of the oligomers in live cells, even though it is cleaved and translocates to the OMM at the initiation of apoptosis. Therefore, we utilized confocal microscopy to measure Förster resonance energy transfer (FRET) efficiencies in live cells to determine the conformation(s) and intermolecular contacts of Bid within these Bcl-2 oligomers. We found that Bid adopts an extended conformation, which appears to be critical for its association with the mitochondrial membrane. This conformation is also important for intermolecular contacts within the Bid oligomer. More importantly for the first time, direct intermolecular contacts between Bid and Bax were observed, thereby, confirming Bid as a key component of these oligomers. Furthermore, the observed FRET efficiencies allowed us to propose an oligomeric arrangement of Bid, Bax, and possibly other members of the Bcl-2 family of proteins that form a self-propagating network that permeabilizes the OMM.

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“…In the absence or saturation of pro-survival Bcl-2 proteins, PUMA can directly activate BAX/BAK to resume the apoptosis process starting from MOMP formation, but this needs further studies to be ascertained [61]. p21, also known as p21 WAF1/Cip1 , regulates negatively the progress of cell division mainly through the inhibition of cyclin-dependent kinases (CDKs) or proliferating cell nuclear antigen (PCNA) as illustrated in Figure 3.…”

Section: Cell Cycle Progress As Affected By Aflatoxin-induced P53 Genmentioning

confidence: 99%

Chronic and Acute Toxicities of Aflatoxins: Mechanisms of Action

Benkerroum

2020

IJERPH

281

214

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There are presently more than 18 known aflatoxins most of which have been insufficiently studied for their incidence, health-risk, and mechanisms of toxicity to allow effective intervention and control means that would significantly and sustainably reduce their incidence and adverse effects on health and economy. Among these, aflatoxin B1 (AFB1) has been by far the most studied; yet, many aspects of the range and mechanisms of the diseases it causes remain to be elucidated. Its mutagenicity, tumorigenicity, and carcinogenicity—which are the best known—still suffer from limitations regarding the relative contribution of the oxidative stress and the reactive epoxide derivative (Aflatoxin-exo 8,9-epoxide) in the induction of the diseases, as well as its metabolic and synthesis pathways. Additionally, despite the well-established additive effects for carcinogenicity between AFB1 and other risk factors, e.g., hepatitis viruses B and C, and the hepatotoxic algal microcystins, the mechanisms of this synergy remain unclear. This study reviews the most recent advances in the field of the mechanisms of toxicity of aflatoxins and the adverse health effects that they cause in humans and animals.

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Bax/Bak activation in the absence of Bid, Bim, Puma, and p53

Cited by 56 publications

References 62 publications

Integrin-β4 is a novel transcriptional target of TAp73

Integrin-β4 is a novel transcriptional target of TAp73

Bcl-2 proteins bid and bax form a network to permeabilize the mitochondria at the onset of apoptosis

Chronic and Acute Toxicities of Aflatoxins: Mechanisms of Action

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