AKT Promotes rRNA Synthesis and Cooperates with c-MYC to Stimulate Ribosome Biogenesis in Cancer

Joanna C. Chan, Katherine M. Hannan, Kim Riddell, Pui Yee Ng, Abigail Peck, Rachel S. Lee, Sandy Hung, Megan V. Astle, Megan Bywater, Meaghan Wall, Gretchen Poortinga, Katarzyna Jastrzebski, Karen E. Sheppard, Brian A. Hemmings, Michael N. Hall, Ricky W. Johnstone, Grant A. McArthur, Ross D. Hannan,* Richard B. Pearson*

*To whom correspondence should be addressed. E-mail: rick.pearson{at}petermac.org (R.B.P.); ross.hannan{at}petermac.org (R.D.H.)

This PDF file includes:

• Materials and Methods
• Fig. S1. AKTi-1/2 inhibits AKT activity in HEK293 and BJ-T cells.
• Fig. S2. AKTi-1/2 represses rDNA transcription and rRNA processing.
• Fig. S3. Knockout of AKT isoforms reduces rDNA transcription.
• Fig. S4. Overexpression of MyrAKT3 increases cell size and serum starvation induces cell cycle arrest without changing apoptosis rates.
• Fig. S5. Knockdown of raptor mimics the effect of rapamycin on RNA Pol I loading.
• Fig. S6. Overexpression of MyrAKT3 increases the abundance of the ribosomal subunits 40S, 60S, and 80S.
• Fig. S7. AKT does not modulate c-MYC abundance or activity and c-MYC does not modulate AKT abundance.
• Fig. S8. Model of regulation of 45S synthesis by AKT, mTORC1, and c-MYC.
• Fig. S9. Cells isolated from Eμ-Myc B cell lymphomas respond to inhibitors of AKT and mTORC1.
• Table S1. Quantitation for Fig. 1A.
• Table S2. Quantitation for Fig. 1C.
• Table S3. Quantitation for Fig. 2B.
• Table S4. Quantitation for Fig. 2C.
• Table S5. Quantitation for Fig. 3C.
• Table S6. Quantitation for Fig. 4B.
• Table S7. Quantitation for Fig. 4C.
• Table S8. Quantitation for Fig. 5B.
• Table S9. Quantitation for fig. S3A.
• Table S10. Quantitation for fig. S9A.
• Table S11. Cloning primers.
• Table S12. RT-PCR primers.
• References
  

[Download PDF]

Technical Details

Format: Adobe Acrobat PDF

Size: 3.8 MB

© 2011 American Association for the Advancement of Science