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TFDP3 inhibits E2F1-induced, p53-mediated apoptosis.

Abstract：

:By dimerizing with E2F proteins, TFDP has profound influence on cellular E2F activities. While TFDP1 and 2 enhance the DNA binding and the transcriptional activity of E2F, the newly identified member of the DP family, TFDP3 primarily functions as a negative regulator. To further characterize the inhibitory property of TFDP3, the present study specifically examined the modulatory role of TFDP3 on E2F1-induced cell death. HEK-293 cells underwent apoptosis following ectopic expression of E2F1. This effect was virtually abolished by co-transfection with TFDP3. In the meantime, the accumulation of p53 proteins and the increased expression of the pro-apoptotic molecules, including Bax, Puma, Noxa, and Bid were found to be suppressed. These data suggest a new mechanism for the regulation of E2F1-induced apoptosis and provide further evidence for the general involvement of TFDP3 in the regulation of E2F functions.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Tian C,Lv D,Qiao H,Zhang J,Yin YH,Qian XP,Wang YP,Zhang Y,Chen WF

doi

10.1016/j.bbrc.2007.06.128

subject

Has Abstract

pub_date

2007-09-14 00:00:00

pages

20-5

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)01347-2

journal_volume

361

pub_type

杂志文章

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