IndraLab

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AKT phosphorylates GATA1. 10 / 12
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"PI3K and AKT stimulates the phosphorylation and activation of GATA1 [XREF_BIBR], and activated GATA-1 upregulates its own gene expression through positive feedback regulation [XREF_BIBR]."

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"Among its pleiotropic effects on erythroid cells, EPO-induced Akt activation promotes differentiation because Akt phosphorylates and activates GATA1 , providing a possible explanation for our observation that inhibition of Akt activity is associated with truncated differentiation."

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"AKT phosphorylates GATA-1 in erythroid cells xref and K562 cells xref resulting in an increase in its DNA-binding affinity and enhanced transcriptional activity."

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"It has been reported that the activation of the PI3K/AKT pathway induces the phosphorylation of GATA-1 (Zhao et al., 2006)."

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"AKT has previously been shown to induce TIMP-1 expression by directly phosphorylating and activating GATA1."

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"Therefore, these results suggest that gastrodin stimulates the PI3K/AKT pathway and that activation of the PI3K/AKT pathway promotes USP4 expression by enhancing the phosphorylation of GATA1 in HepG2 cells."

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"AKT phosphorylates GATA-1 in erythroid cells XREF_BIBR and K562 cells XREF_BIBR resulting in an increase in its DNA binding affinity and enhanced transcriptional activity."

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"Here, we show that erythropoietin activates AKT, which phosphorylates GATA-1 at Ser310, thereby increasing GATA-1 affinity for FOG-1."

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"Of these, JAK2-STAT5 activates Bcl-xL to prevent apoptosis of erythroid progenitors, whereas Akt promotes differentiation by phosphorylating the essential erythroid transcription factor GATA1 and activating metabolic pathways via phosphorylation of the mTORC1 complex."

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"Among its pleiotropic effects on erythroid cells, EPO induced Akt activation promotes differentiation because Akt phosphorylates and activates GATA1, providing a possible explanation for our observation that inhibition of Akt activity is associated with truncated differentiation."
AKT phosphorylates GATA1 on S310. 10 / 11
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"It has been reported that Akt directly phosphorylated GATA1 at serine 310 [ xref ], and PAK5 was in higher expression in breast cancer tissues than matched adjacent noncancerous tissues."

"We found that akt directly phosphorylates the transcription factor gata-1 at serine 310 and that this site-specific phosphorylation is required for the transcriptional activation of the timp-1 promoter."

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"It has also been reported that Akt dependent phosphorylation of GATA-1 at serine 310 is necessary for EPO induced erythrocyte terminal differentiation in a proerythroblast cell line XREF_BIBR and for EPO induced TIMP1 secretion and maturation of fetal liver erythroid cells XREF_BIBR."

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"AKT serine threonine kinase phosphorylates GATA-1S310 in vitro and in erythroid cells and enhances GATA-1 transcriptional activity."

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"AKT phosphorylates GATA-1 at Ser 310 and enhances its transcriptional activity in primary fetal liver cells (42)."

No evidence text available

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"AKT phosphorylates GATA-1 at Ser-310 and enhances its transcriptional activity in primary fetal liver cells (42) ."

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"Here, we show that erythropoietin activates AKT, which phosphorylates GATA-1 at Ser310, thereby increasing GATA-1 affinity for FOG-1."

sparser
"It has also been reported that Akt-dependent phosphorylation of GATA-1 at serine 310 is necessary for EPO-induced erythrocyte terminal differentiation in a proerythroblast cell line xref and for EPO-induced TIMP1 secretion and maturation of fetal liver erythroid cells xref ."

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"Here, we show that erythropoietin activates AKT, which phosphorylates GATA-1 at Ser310, thereby increasing GATA-1 affinity for FOG-1."
Kinase-active AKT leads to the phosphorylation of GATA1 on serine. 1 / 1
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"The PI3-kinase/AKT signaling pathway is identified as a mediator of Epo-induced phosphorylation of GATA-1. AKT serine threonine kinase phosphorylates GATA-1S310 in vitro and in erythroid cells and enhances GATA-1 transcriptional activity. "
Kinase-active AKT phosphorylates GATA1 on S310. 1 / 1
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"PhosphoElm data from PMID 15212693"
AKT phosphorylates GATA1 on S26. 1 / 1
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"GATA1 can be strongly phosphorylated at residue Ser26 of the N-terminal acidic activation domain by MAPK and at Ser310 of the DNA binding domain by Akt in response to growth factors such as Epo."