| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10802793 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2011 | 12 Pages |
Abstract
⺠AKT binding to FoxO3 is independent of the RxRxxS/T AKT phosphorylation recognition motif. ⺠AKT activation is required for FoxO3 binding. ⺠AKT expression increases FoxO3 steady-state protein levels. ⺠14â3â3 binding stabilizes phosphorylated FoxO3. ⺠FoxO3 P34A mutation impairs 14â3â3 binding, resulting in a constitutively active form.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Melissa Dobson, Gopalakrishnan Ramakrishnan, Stephanie Ma, Ludmila Kaplun, Vitaly Balan, Rafael Fridman, Guri Tzivion,