IndraLab

Statements


FOXO1 phosphorylated on S256 is transcriptionally inactive. 3 / 3
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"Insulin disrupts IRS-dependent transactivation by FKHR, and phosphorylation of Ser-256 by PKB is necessary and sufficient to mediate this effect."

"We found that the phosphorylation of Ser-256 and introduction of a negative charge at this site (by replacing Ser-256 with an aspartate) also inhibits transactivation by FKHR, even when the phosphorylation of Thr-24 and Ser-319 has been prevented by replacing these residues with alanine."

"FKHR is phosphorylated by protein kinase B (PKB) at Thr24, Ser256 and Ser319 in response to growth factors, stimulating the nuclear exit and inactivation of this transcription factor."