IndraLab

Statements


TP53 phosphorylated on S46 is transcriptionally active. 14 / 14
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"Recent studies revealed that phosphorylation of p53 on Ser(46) was associated with induction of p53AIP1 expression, resulting in the commitment of the cell fate into apoptotic cell death."

"Co-exposure to C75 and Taxol induced a remarkable nuclear accumulation of activated p38 mitogen-activated protein kinase (p38 MAPK), which was accompanied by a synergistic nuclear accumulation of the p53 tumor-suppressor protein that was phosphorylated at Ser46, a p38 MAPK-regulated pro-apoptotic modification of p53"

"HIPK2 is activated by ultraviolet (UV) radiation and selectively phosphorylates p53 at Ser 46 ... Accordingly, the kinase function of HIPK2 mediates the increased expression of p53 target genes"

"Mutation of p53 Ser(58) (equivalent to human p53 Ser(46)) abrogates transcription of these genes"

"Through direct cloning of p53 binding sequences from human genomic DNA, we have isolated a novel gene, designated p53AIP1 (p53-regulated Apoptosis-Inducing Protein 1), whose expression is inducible by wild-type p53. Ectopically expressed p53AIP1, which is localized within mitochondria, leads to apoptotic cell death through dissipation of mitochondrial A(psi)m. We have found that upon severe DNA damage, Ser-46 on p53 is phosphorylated and apoptosis is induced. In addition, substitution of Ser-46 inhibits the ability of p53 to induce apoptosis and selectively blocks expression of p53AIP1. Our results suggest that p53AIP1 is likely to play an important role in mediating p53-dependent apoptosis, and phosphorylation of Ser-46 regulates the transcriptional activation of this apoptosis-inducing gene."

"Here we demonstrate that homeodomain-interacting protein kinase-2 (HIPK2), a member of a novel family of nuclear serine/threonine kinases, binds to and activates p53 by directly phosphorylating it at Ser 46"

"Here we demonstrate that homeodomain-interacting protein kinase-2 (HIPK2), a member of a novel family of nuclear serine/threonine kinases, binds to and activates p53 by directly phosphorylating it at Ser 46"

"Recent studies revealed that phosphorylation of p53 on Ser(46) was associated with induction of p53AIP1 expression, resulting in the commitment of the cell fate into apoptotic cell death."

"TP53INP1 mediates phosphorylation of p53 on serine 46 (S46). ASPP-1 and ASPP-2 modulate the cellular apoptotic threshold by direct interaction with p53, thereby enhancing the DNA binding and trans-activation function of p53 on the promoters of pro-apoptotic genes in vivo"

"TP53INP1 mediates phosphorylation of p53 on serine 46 (S46). ASPP-1 and ASPP-2 modulate the cellular apoptotic threshold by direct interaction with p53, thereby enhancing the DNA binding and trans-activation function of p53 on the promoters of pro-apoptotic genes in vivo"

"Through direct cloning of p53 binding sequences from human genomic DNA, we have isolated a novel gene, designated p53AIP1 (p53-regulated Apoptosis-Inducing Protein 1), whose expression is inducible by wild-type p53. Ectopically expressed p53AIP1, which is localized within mitochondria, leads to apoptotic cell death through dissipation of mitochondrial A(psi)m. We have found that upon severe DNA damage, Ser-46 on p53 is phosphorylated and apoptosis is induced. In addition, substitution of Ser-46 inhibits the ability of p53 to induce apoptosis and selectively blocks expression of p53AIP1. Our results suggest that p53AIP1 is likely to play an important role in mediating p53-dependent apoptosis, and phosphorylation of Ser-46 regulates the transcriptional activation of this apoptosis-inducing gene."

"Co-exposure to C75 and Taxol induced a remarkable nuclear accumulation of activated p38 mitogen-activated protein kinase (p38 MAPK), which was accompanied by a synergistic nuclear accumulation of the p53 tumor-suppressor protein that was phosphorylated at Ser46, a p38 MAPK-regulated pro-apoptotic modification of p53"

"Mutation of p53 Ser(58) (equivalent to human p53 Ser(46)) abrogates transcription of these genes"

"HIPK2 is activated by ultraviolet (UV) radiation and selectively phosphorylates p53 at Ser 46 ... Accordingly, the kinase function of HIPK2 mediates the increased expression of p53 target genes"