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Sci. Signal., 11 June 2013
[DOI: 10.1126/scisignal.2004015]

Supplementary Materials for:

AKT Facilitates EGFR Trafficking and Degradation by Phosphorylating and Activating PIKfyve

Ekrem Emrah Er, Michelle C. Mendoza, Ashley M. Mackey, Lucia E. Rameh, John Blenis*

*Corresponding author. E-mail: jblenis{at}hms.harvard.edu

This PDF file includes:

  • Fig. S1. Stimulation with high EGF concentrations induces lysosomal degradation of EGFR independently of EGFR abundance.
  • Fig. S2. Internalization of EGF/EGFR does not require AKT activity.
  • Fig. S3. RAB11a knockdown reduces the rate of EGFR degradation.
  • Fig. S4. EGFR recycling assay.
  • Fig. S5. Effects of AKTVIII on the colocalization of EGF with LAMP2.
  • Fig. S6. SAC3 promotes EGFR degradation but is not regulated by AKT.
  • Fig. S7. The PIKfyve-ArPIKfyve-SAC3 complex promotes EGFR degradation.
  • Fig. S8. PIKfyve and AKT promote PDGFRβ degradation in HMECs.
  • Fig. S9. AKT reduces EGFR signaling to ERK.

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Technical Details

Format: Adobe Acrobat PDF

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Citation: E. E. Er, M. C. Mendoza, A. M. Mackey, L. E. Rameh, J. Blenis, AKT Facilitates EGFR Trafficking and Degradation by Phosphorylating and Activating PIKfyve. Sci. Signal. 6, ra45 (2013).

© 2013 American Association for the Advancement of Science


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