This PDF file includes:

• Fig. S1. KHK-A is required for oxidative stress–enhanced p62 oligomerization.
• Fig. S2. KHK-A is required for Nrf2 activation upon oxidative stress.
• Fig. S3. AMPK phosphorylates KHK-A and promotes the association between KHK-A and p62.
• Fig. S4. AMPK-mediated KHK-A S80 phosphorylation inhibits the interaction between KHK-A and PRPS1 and PRPS1 T225 phosphorylation.
• Fig. S5. KHK-A acts as a protein kinase and phosphorylates p62 at S28.
• Fig. S6. KHK-A is required for oxidative stress–induced but not proteasomal stress−induced p62 aggregation.
• Fig. S7. KHK-A–mediated p62 S28 phosphorylation is required for oxidative stress–enhanced p62 oligomerization and Nrf2 activation.
• Fig. S8. KHK-A mediated p62 S28 phosphorylation reduces ROS production and promotes cancer cell survival without altering autophagy initiation.
• Fig. S9. The phosphorylation-mimicking KHK-A S80E and p62 S28E mutations promote p62 oligomerization and Nrf2 activation.
• Fig. S10. KHK-A–mediated p62 S28 phosphorylation promotes hepatocellular tumorigenesis and is associated with the clinical aggressiveness of human HCC.

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