E2F proteins

Loughran, Oonagh; Thangué, Nicholas B. La

doi:10.1016/s0960-9822(02)00876-x

Cited by 3 publications

(2 citation statements)

References 3 publications

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“…5 The tumor suppressor pRb (retinoblastoma susceptibility protein) arrests cell cycle progression by binding E2F1, E2F2, and E2F3 and inhibiting their transcriptional activity, whereas p107 binds E2F4 and p130 binds E2F5 to inhibit cell proliferation. 6 Like pRb, p53 only binds E2F1-3 due to the presence of a conserved domain in the N-terminus, which is not present in the other family members. Moreover, the p53-binding domain in E2F1-3 also binds cyclin A.…”

Section: The E2f Familymentioning

confidence: 99%

Some p53-binding proteins that can function as arbiters of life and death

2006

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Four sets of p53-binding proteins are discussed in this review. These are the E2F family, the ASPP family, Y-boxbinding protein YB1, and the prolyl isomerase Pin1. Each appears to play a role in the decision by p53 to induce an arrest of cell proliferation or apoptosis and they may also be independent markers of cancer. Their activities appear to be linked with the cell cycle and they may also interact with each other. In this review, the properties of each protein class are discussed as well as how they affect p53 functions. A model is proposed as to how their activities might be coordinated.

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Section: The E2f Familymentioning

confidence: 99%

Some p53-binding proteins that can function as arbiters of life and death

2006

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“…The E2F family of transcription factors is a key factor in the regulation of cell proliferation (Zwicker and Mu¨ller, 1996;Muller and Helin, 2000;Nevins, 2001;Phillips and Vousden, 2001;Loughran and La Thangue, 2002). E2F transcription factors are heterodimeric proteins consisting of one member of the E2F family and one member of the DP family.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of cell proliferation and induction of apoptosis by novel tetravalent peptides inhibiting DNA binding of E2F

2003

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We have isolated several peptides from random peptide phage display libraries that specifically recognize the cell cycle regulatory transcription factor E2F and inhibit DNA binding of E2F/DP heterodimers (E2F-1, E2F-2, E2F-3, E2F-4 or E2F-5, and DP-1). The inhibitory efficiency could be strongly enhanced by generating branched tetravalent molecules. To analyse the biological consequences of peptide-mediated E2F inhibition, we fused two of these branched molecules to a cell-penetrating peptide derived from the HTV-Tat protein. Incubation of human tumor cells with these branched Tat-containing peptides led to an inhibition of cell proliferation and induction of apoptosis. These results provide new insights into the function of E2F and further validate E2F as a potential therapeutic target in proliferative diseases.

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