Supplementary Materials

Supplementary Materials for:

Acetylation-dependent regulation of MDM2 E3 ligase activity dictates its oncogenic function

Naoe T. Nihira, Kohei Ogura, Kouhei Shimizu, Brian J. North, Jinfang Zhang, Daming Gao, Hiroyuki Inuzuka,* Wenyi Wei*

*Corresponding author. Email: wwei2{at}bidmc.harvard.edu (W.W.); hinuzuka{at}bidmc.harvard.edu (H.I.)

This PDF file includes:

  • Fig. S1. p300 promotes MDM2 acetylation largely at the Lys182 and Lys185 residues.
  • Fig. S2. Sirtuin family of deacetylases governs MDM2 acetylation status in cells.
  • Fig. S3. MDM2 acetylation status affects its intra- and intermolecular interaction with MDM2 interacting proteins.
  • Fig. S4. Acetylation of MDM2 governs the intramolecular interaction between its functional domains, as well as the intermolecular interaction between MDM2 and HAUSP.
  • Fig. S5. HAUSP interaction with MDM2 is independent of nuclear translocation of MDM2.
  • Fig. S6. Acetylation of MDM2 enhances the oncogenic function of MDM2.

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Citation: N. T. Nihira, K. Ogura, K. Shimizu, B. J. North, J. Zhang, D. Gao, H. Inuzuka, W. Wei, Acetylation-dependent regulation of MDM2 E3 ligase activity dictates its oncogenic function. Sci. Signal. 10, eaai8026 (2017).

© 2017 American Association for the Advancement of Science