Regulation of Epidermal Growth Factor Receptor Trafficking by Lysine Deacetylase HDAC6

Yonathan Lissanu Deribe, Philipp Wild, Akhila Chandrashaker, Jasna Curak, Mirko H. H. Schmidt, Yannis Kalaidzidis, Natasa Milutinovic, Irina Kratchmarova, Lukas Buerkle, Michael J. Fetchko, Philipp Schmidt, Saranya Kittanakom, Kevin R. Brown, Igor Jurisica, Blagoy Blagoev, Marino Zerial, Igor Stagljar,* Ivan Dikic*

*To whom correspondence should be addressed. E-mail: Ivan.Dikic{at}biochem2.de (I.D.) and igor.stagljar{at}utoronto.ca (I.S.)

This PDF file includes:

• Fig. S1. Generation and characterization of EGFR bait construct.
• Fig. S2. Integrating EGFR-interacting proteins from multiple data sets.
• Fig. S3. Validation of EGFR-interacting proteins identified in the MYTH screen.
• Fig. S4. HDAC6 interacts with EGFR.
• Fig. S5. HDAC6 interacts with other ErbB family members, but not with mammalian integral membrane transporters and ion channels.
  Fig. S6. HDAC6 overexpression increases the abundance of EGFR.
• Fig. S7. HDAC6 and EGFR partially colocalize at the plasma membrane, and in a fraction of intracellular vesicles following EGF stimulation.
• Fig. S8. Downregulation of HDAC6 changes characteristics of endosomes.
• Fig. S9. HSP90 inhibition has no discernible effect on ligand-induced degradation of EGFR.
• Fig. S10. Identification of tubulin Lys⁴⁰ acetylation by mass spectrometry.
• Tables S1 to S7. Annotation of EGFR-interacting proteins identified in MYTH and comparison to prior studies.
• Movie S1 Legend. Live cell imaging of A431 cells stably expressing GFP-Rab5.
• References

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Other Supplementary Material for this manuscript includes the following:

• Movie S1 (.mp4 format)
• NAViGaTOR file for Figure 1A (.xml format)

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