Association of Purα and E2F-1 suppresses transcriptional activity of E2F-1

Darbinian, Nune; Gallia, Gary L.; Kundu, Mondira; Shcherbik, Natalia; Tretiakova, Anna P.; Giordano, Antonio; Khalili, Kamel

doi:10.1038/sj.onc.1203011

Cited by 53 publications

(44 citation statements)

References 18 publications

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“…In addition, interaction of these proteins with other factors has been shown to modify their DNA binding abilities. Interaction of the PUR protein with factors such as retinoblastoma protein (Rb), E2F-1, cyclin A, and YB-1 has been shown to attenuate its DNA binding ability (26,33,34). Conversely, interaction of PUR␣ with Ca 2ϩ /calmodulin has been shown to augment its DNA binding ability to the recognition sequence (35).…”

Section: Discussionmentioning

confidence: 99%

Single-stranded DNA-binding Proteins PURα and PURβ Bind to a Purine-rich Negative Regulatory Element of the α-Myosin Heavy Chain Gene and Control Transcriptional and Translational Regulation of the Gene Expression

Gupta

Sueblinvong

Raman

et al. 2003

Journal of Biological Chemistry

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The ␣-myosin heavy chain is a principal molecule of the thick filament of the sarcomere, expressed primarily in cardiac myocytes. The mechanism for its cardiacrestricted expression is not yet fully understood. We previously identified a purine-rich negative regulatory (PNR) element in the first intron of the gene, which is essential for its cardiac-specific expression (Gupta, M., Zak, R., Libermann, T. A., and Gupta, M. P.

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Section: Discussionmentioning

confidence: 99%

Single-stranded DNA-binding Proteins PURα and PURβ Bind to a Purine-rich Negative Regulatory Element of the α-Myosin Heavy Chain Gene and Control Transcriptional and Translational Regulation of the Gene Expression

Gupta

Sueblinvong

Raman

et al. 2003

Journal of Biological Chemistry

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“…More recently, Pur␣ has been revealed to be an RNA binding protein with potential effects on translation (28). Analysis of the predicted 322-amino-acid human Pur␣ protein has revealed a modular structure with alternating 23-and 26-amino-acid repeats (3) which are important for Pur␣ binding to DNA while other regions of the protein contribute by binding to several cellular regulatory proteins, including SP1 (47), YB-1 (42), E2F-1 (10), and pRb (25). Colocalizations of Pur␣ with cyclin A/Cdk2 and cyclin B1/Cdk1 have been reported (1), and unpublished work suggests that these are mediated by binding to the Cdk component (S. Barr, H. Liu, and E. M. Johnson, unpublished data).…”

mentioning

confidence: 99%

Purα Is Essential for Postnatal Brain Development and Developmentally Coupled Cellular Proliferation As Revealed by Genetic Inactivation in the Mouse

Khalili

Valle

Muralidharan

et al. 2003

Molecular and Cellular Biology

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“…The best studied mechanism involves the blockade of E2F transactivation domain by RB binding (39 -40). Additionally, inhibition of E2F binding to DNA, as observed on interaction of E2F1 and Pur␣ (41), is also known to negatively affect the activity of E2Fs. Our data suggests that the formation of a DNA-bound ALY/E2F2 complex, similar to the recently described p14ARF-E2F/partner-DNA super complex (42), is responsible for the inhibition of E2F2 activity.…”

Section: Modulation Of E2f2-dependent Transcriptionalmentioning

confidence: 99%

The Nuclear Protein ALY Binds to and Modulates the Activity of Transcription Factor E2F2

Osinalde

Olea

Mitxelena

et al. 2013

Molecular & Cellular Proteomics

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E2F transcription factors control the expression of genes involved in a variety of essential cellular processes and consequently their activity needs to be tightly regulated. Protein-protein interactions are thought to be key modulators of E2F activity. To gain insight into the mechanisms that regulate the activity of E2F2, we searched for novel proteins that associate with this transcription factor. We show that the nuclear protein ALY (THO complex 4), originally described as a transcriptional co-activator, associates with DNA-bound E2F2 and represses its transcriptional activity. The capacity of ALY to modulate gene expression was analyzed with expression microarrays by characterizing the transcriptome of E2F2 expressing HEK293T cells in which ALY was either overexpressed or silenced. We show that ALY influences the expression of more than 400 genes, including 98 genes bearing consensus E2F motifs. Thus, ALY emerges as a novel E2F2-interacting protein and a relevant modulator of E2F-responsive gene expression. Molecular & Cellular

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Association of Purα and E2F-1 suppresses transcriptional activity of E2F-1

Cited by 53 publications

References 18 publications

Single-stranded DNA-binding Proteins PURα and PURβ Bind to a Purine-rich Negative Regulatory Element of the α-Myosin Heavy Chain Gene and Control Transcriptional and Translational Regulation of the Gene Expression

Single-stranded DNA-binding Proteins PURα and PURβ Bind to a Purine-rich Negative Regulatory Element of the α-Myosin Heavy Chain Gene and Control Transcriptional and Translational Regulation of the Gene Expression

Purα Is Essential for Postnatal Brain Development and Developmentally Coupled Cellular Proliferation As Revealed by Genetic Inactivation in the Mouse

The Nuclear Protein ALY Binds to and Modulates the Activity of Transcription Factor E2F2

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