TFDP3 inhibits E2F1-induced, p53-mediated apoptosis.
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.
Tian
Chan
C
Department of Immunology, Peking University Health Science Center, 38 Xue Yuan Road, Beijing 100083, China.
Lv
Dan
D
Qiao
Huan
H
Zhang
Jun
J
Yin
Yan-hui
YH
Qian
Xiao-ping
XP
Wang
Yu-ping
YP
Zhang
Yu
Y
Chen
Wei-feng
WF
D017209:Apoptosis; D002460:Cell Line; D050687:E2F1 Transcription Factor / Q000037:antagonists & inhibitors*; D005720:Gamma Rays; D006801:Humans; D050680:Transcription Factor DP1 / Q000502:physiology*; D016159:Tumor Suppressor Protein p53 / Q000037:antagonists & inhibitors*
D050687:E2F1 Transcription Factor; C516920:TFDP3 protein, human; D050680:Transcription Factor DP1; D016159:Tumor Suppressor Protein p53