Adenovirus E1A activation domain binds the basic repeat in the TATA box transcription factor

Lee, Wes S.; Kao, C. Y.; Bryant, Gene O.; Li, Xuan; Berk, Arnold

doi:10.1016/0092-8674(91)90188-5

Cited by 377 publications

(327 citation statements)

References 50 publications

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“…For example, the Rb family of transcriptional corepressors bind to CR1 and CR2, the CBP/p300 family of acetyltransferases bind to the N-terminal region and CR1, whereas CtBP1 and CtBP2 associate with the C-terminal CR4 domain (Whyte et al, 1989;Dyson et al, 1992;Boyd et al, 1993;Eckner et al, 1994;Arany et al, 1995). CR3, exclusive to the E1A13S protein, binds to proteins involved in transcriptional activation, such as TATA binding protein (TBP), Mediator 23 (Med23) and associated transcription factors (ATFs), various transcription factors and proteasome components (Lee et al, 1991;Green, 1990, 1994;Geisberg et al, 1994Geisberg et al, , 1995Boyer et al, 1999;Wang and Berk, 2002;Rasti et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Adenovirus 5 E1A is responsible for increased expression of insulin receptor substrate 4 in established adenovirus 5-transformed cell lines and interacts with IRS components activating the PI3 kinase/Akt signalling pathway

et al. 2008

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Using mass spectrometric analysis insulin receptor substrate 4 (IRS-4) has been identified as a novel adenovirus 5 early region 1A (Ad5E1A)-binding protein. IRS-4 interacts with both the transcriptional activation domain (conserved region 3) and the N-terminal region of Ad5E1A13S. Prolonged expression of Ad5E1A13S is required for the observed dramatic increase in the levels of IRS-4 mRNA and protein in Ad5E1-transformed human cell lines. Once expressed, as well as binding to E1A and the insulin receptor, IRS-4 remains tyrosine phosphorylated and constitutively associates with the regulatory p85 subunit of phosphoinositide 3 kinase, resulting in the phosphorylation of Akt (causing activation) and GSK-3b (causing inhibition). Reducing IRS-4 expression using small interfering RNA (siRNA) in established Ad5E1A-expressing cell lines decreases the activation of Akt and cellular proliferation. During Ad5 infection, IRS-4 is not expressed. However, Ad5E1A associates with IRS-1, increasing Akt and GSK-3b phosphorylation and tyrosine phosphorylation of IRS-1 itself. We conclude that the association and altered regulation of IRS proteins by Ad5E1A contribute to the adenovirus-transformed phenotype and modulates viral infection in an Akt-dependent manner.

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Section: Introductionmentioning

confidence: 99%

Adenovirus 5 E1A is responsible for increased expression of insulin receptor substrate 4 in established adenovirus 5-transformed cell lines and interacts with IRS components activating the PI3 kinase/Akt signalling pathway

et al. 2008

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“…38,39 In addition, the CR3 domain is involved in transcription activation. The CR3 domain consists of two distinct activities: the N-terminal part is a strong transcription activator and interacts with TATA-binding protein TFIID; 28,40 the C-terminal portion has a promoter binding function which is required to direct the E1A protein to some natural targets, such as the ATF-2. 41 CR3 thus activates transcription by forming an adapter mediating the interaction between the sequence-specific DNA binding transcription factor and the TATA box-binding protein.…”

Section: Discussionmentioning

confidence: 99%

Safety study and characterization of E1A–liposome complex gene-delivery protocol in an ovarian cancer model

et al. 1998

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A phase I clinical trial of E1A-liposome complex is curcantly reduce any potential adverse effects caused by lipid rently ongoing in patients with HER-2/neu-overexpressing vector and E1A DNA. To examine further whether residual breast or ovarian cancers. To optimize the E1A-liposome E1A DNA may still exist in normal organs after the E1A-complex for a further stage of clinical trial, several aspects liposome treatment, PCR was used to detect E1A DNA in of the current protocol have been examined in an animal mice that survived for 1. years after the last treatment. E1A model. In the orthotopic ovarian cancer model, different DNA was detected only in the lungs and kidneys, but not doses of lipid in the the E1A-liposome complex, which is in livers, hearts, spleens, brains, uterus or the ovaries. Furcurrently used in clinical trials, were tested for the in vivo thermore, resistance of the E1A DNA extracted from gene-transfer efficacy and tumor-suppression function. A tissues to the digestion of DpnI restriction enzyme, which lowered lipid dose -1/13 of the previous amount -procan cleave the methylated E1A plasmid DNA generated by duced gene expression level and E1A tumor-suppression methylation-competent bacteria, suggested integration of efficacy similar to that of the original protocol. Mini-E1A, an E1A DNA into the chromosome of the lungs and kidneys. E1A construct without its immortalization domain and yetExperimental results presented here provide important capable of repressing HER-2/neu, was proved to be as information for safety concerns and for the design of future potent as E1A in suppressing tumor development in vivo.phase II and phase III trials. These changes in the E1A-liposome complex will signifi-

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“…For example, adenovirus EIA was shown to increase expression of the hsp70 gene by stimulating the promoter activity [22]. The mechanism of EIA·activation has been studied by analyzing the hsp70 promoter [24][25][26][27]. It has been shown that both the TATA' and the 'CAAT' elements in the hsp70 promoter are targets of EIA·activation [25][26][27].…”

Section: Discussionmentioning

confidence: 99%

“…Consistently. it has been also shown that EIA associates with the 'TATA'·binding factor TBP [25,26] and 'CAAT'·binding factor CTF [27]. The interaction between EIA and TBP or CTF largely involves the conserved region 3 of the EIA protein.…”

Section: Discussionmentioning

confidence: 99%

HPV 16 E7 oncoprotein induces expression of a 110 kDa heat shock protein

1995

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Heat shock protein genes are induced by various kinds of stress. Besides stress, the heat shock family gene hsp70 has been shown to be induced by growth-stimulating agents such as the DNA virus oncoproteins and serum. Here, we report cloning of a novel cDNA that encodes a 100 kDa heat shock proteinrelated polypeptide as a human papillomavirus oncoprotein E7-inducible gene. E7 induces expression of this heat shock protein at the level of RNA synthesis. Moreover, the induction of this heat shock protein-mRNA was dependent on the conserved region 2 of the E7 protein, which is essential for binding to the proteins of the retinoblastoma family.

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Adenovirus E1A activation domain binds the basic repeat in the TATA box transcription factor

Cited by 377 publications

References 50 publications

Adenovirus 5 E1A is responsible for increased expression of insulin receptor substrate 4 in established adenovirus 5-transformed cell lines and interacts with IRS components activating the PI3 kinase/Akt signalling pathway

Adenovirus 5 E1A is responsible for increased expression of insulin receptor substrate 4 in established adenovirus 5-transformed cell lines and interacts with IRS components activating the PI3 kinase/Akt signalling pathway

Safety study and characterization of E1A–liposome complex gene-delivery protocol in an ovarian cancer model

HPV 16 E7 oncoprotein induces expression of a 110 kDa heat shock protein

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