Supplementary Materials

Supplementary Materials for:

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

Yixin Yao, Milind Suraokar, Bryant G. Darnay, Brett G. Hollier, Tattym E. Shaiken, Takayuki Asano, Chien-Hung Chen, Benny H.-J. Chang, Yiling Lu, Gordon B. Mills, Dos Sarbassov, Sendurai A. Mani, James L. Abbruzzese, Shrikanth A. G. Reddy*

*To whom correspondence should be addressed. E-mail: sareddy{at}mdanderson.org

This PDF file includes:

  • Fig. S1. Identification of an Akt1-interacting protein.
  • Fig. S2. BSTA (Mr 55,000) interacts with Akt and is phosphorylated in cells.
  • Fig. S3. Akt activity is dispensable for the BSTA-Akt interaction.
  • Fig. S4. Identification of a putative BSTA-binding sequence in Akt1.
  • Fig. S5. Effect of BSTA mutants and siRNA on the phosphorylation status of Akt.
  • Fig. S6. Mechanism of BSTA-mediated phosphorylation of Akt.
  • Fig. S7. Akt multimerization requires BSTA and mTORC2.
  • Fig. S8. BSTA promotes glucose uptake and adipocyte differentiation.
  • Fig. S9. Effects of BSTA, BSTA-AA, BSD, and BSD-AA on adipocyte differentiation.
  • Fig. S10. BSTA, Ser473 in Akt, and FoxC2 regulate adipocyte differentiation.
  • References (59) and (60)

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Citation: Y. Yao, M. Suraokar, B. G. Darnay, B. G. Hollier, T. E. Shaiken, T. Asano, C.-H. Chen, B. H.-J. Chang, Y. Lu, G. B. Mills, D. Sarbassov, S. A. Mani, J. L. Abbruzzese, S. A. G. Reddy, BSTA Promotes mTORC2-Mediated Phosphorylation of Akt1 to Suppress Expression of FoxC2 and Stimulate Adipocyte Differentiation. Sci. Signal. 6, ra2 (2013).

© 2013 American Association for the Advancement of Science