Research ArticleCell Biology

BSTA Promotes mTORC2-Mediated Phosphorylation of Akt1 to Suppress Expression of FoxC2 and Stimulate Adipocyte Differentiation

Science Signaling  08 Jan 2013:
Vol. 6, Issue 257, pp. ra2
DOI: 10.1126/scisignal.2003295

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Akt1 Activator

Activation of the kinase Akt1, which requires phosphorylation at Ser473, promotes adipocyte differentiation, which requires suppression of the gene encoding the transcription factor FoxC2. Yao et al. identified a protein they called BSTA (BSD domain–containing signal transducer and Akt interactor) as a binding partner of Akt1 that enhanced its phosphorylation at Ser473 by mTORC2 (mammalian target of rapamycin complex 2). BSTA promoted phosphorylation of Akt1 in differentiating adipocytes, and embryonic stem cells lacking BSTA failed to differentiate into adipocytes, which was caused by lack of suppression of FoxC2. Thus, these results demonstrate that BSTA is an essential activator of Akt1 during adipocyte differentiation.