TY - JOUR
T1 - Identification of Akt interaction protein PHF20/TZP that transcriptionally regulates p53
AU - Park, Sungman
AU - Kim, Donghwa
AU - Dan, Han C.
AU - Chen, Huihua
AU - Testa, Joseph R.
AU - Cheng, Jin Q.
PY - 2012/3/30
Y1 - 2012/3/30
N2 - Akt regulates a diverse array of cellular functions, including cell survival, proliferation, differentiation, and metabolism. Although a number of molecules have been identified as upstream regulators and downstream targets of Akt, the mechanisms by which Akt regulates these cellular processes remain elusive. Here, we demonstrate that a novel transcription factor, PHF20/TZP (referring to Tudor and zinc finger domain containing protein), binds to Akt and induces p53 expression at the transcription level. Knockdown of PHF20 significantly reduces p53. PHF20 inhibits cell growth, DNA synthesis, and cell survival. Akt phosphorylates PHF20 at Ser291 in vitro and in vivo, which results in its translocation from the nucleus to the cytoplasm and attenuation of PHF20 function. These data indicate that PHF20 is a substrate of Akt and plays a role in Akt cell survival/growth signaling.
AB - Akt regulates a diverse array of cellular functions, including cell survival, proliferation, differentiation, and metabolism. Although a number of molecules have been identified as upstream regulators and downstream targets of Akt, the mechanisms by which Akt regulates these cellular processes remain elusive. Here, we demonstrate that a novel transcription factor, PHF20/TZP (referring to Tudor and zinc finger domain containing protein), binds to Akt and induces p53 expression at the transcription level. Knockdown of PHF20 significantly reduces p53. PHF20 inhibits cell growth, DNA synthesis, and cell survival. Akt phosphorylates PHF20 at Ser291 in vitro and in vivo, which results in its translocation from the nucleus to the cytoplasm and attenuation of PHF20 function. These data indicate that PHF20 is a substrate of Akt and plays a role in Akt cell survival/growth signaling.
UR - http://www.scopus.com/inward/record.url?scp=84859499770&partnerID=8YFLogxK
U2 - 10.1074/jbc.M111.333922
DO - 10.1074/jbc.M111.333922
M3 - Article
C2 - 22334668
AN - SCOPUS:84859499770
SN - 0021-9258
VL - 287
SP - 11151
EP - 11163
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 14
ER -