TIM Family Proteins Promote the Lysosomal Degradation of the Nuclear Receptor NUR77

Savithri Balasubramanian,* Satya Keerthi Kota, Vijay K. Kuchroo, Benjamin D. Humphreys, Terry B. Strom*

*To whom correspondence should be addressed. E-mail: skota{at}bidmc.harvard.edu (S.B.); tstrom{at}bidmc.harvard.edu (T.B.S.)

This PDF file includes:

• Fig. S1. NUR77 domains required for the interaction with TIM-1.
• Fig. S2. TIM proteins do not affect the abundance of GFP.
• Fig. S3. Reduction of NUR77 protein abundance is not through squelching.
• Fig. S4. Silencing of TIM-1 increases NUR77 protein abundance in HK-2 cells in an in vitro epithelial cell injury model.
• Fig. S5. Cellular localization of endogenous TIM-1.
• Fig. S6. The IgV domain of TIM proteins is highly conserved.
• Fig. S7. Localization pattern of wild-type and signal peptide–deleted TIM-1 proteins.
• Fig. S8. The requirement for PI3K in TIM-1–mediated degradation of NUR77 is independent of Akt signaling.
• Fig. S9. TIM-1 is not subjected to lysosomal degradation.
• Fig. S10. Colocalization of NUR77 and TIM-1 with the autophagosome marker LC3.
• Table S1. Interacting partners of hTIM-1 identified in the yeast two-hybrid screen.

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© 2012 American Association for the Advancement of Science