Supplementary Materials for:

Stress-induced dynamic regulation of mitochondrial STAT3 and its association with cyclophilin D reduce mitochondrial ROS production

Jeremy A. Meier, Moonjung Hyun, Marc Cantwell, Ali Raza, Claudia Mertens, Vidisha Raje, Jennifer Sisler, Erin Tracy, Sylvia Torres-Odio, Suzana Gispert, Peter E. Shaw, Heinz Baumann, Dipankar Bandyopadhyay, Kazuaki Takabe, Andrew C. Larner*

*Corresponding author. Email: andrew.larner{at}vcuhealth.org

This PDF file includes:

• Fig. S1. Ser⁷²⁷ and Tyr⁷⁰⁵ of STAT3 are not required for H₂O₂-induced mitoSTAT3 loss.
• Fig. S2. Selectivity of the mitoSTAT3 signaling pathway and relevance in vivo.
• Fig. S3. Inhibition of relevant kinase pathways does not affect stimulation-induced decreases in mitoSTAT3.
• Fig. S4. Inhibition of mitoproteases does not affect proteolysis of mitoSTAT3.
• Fig. S5. mitoSTAT3 inducibly binds to CypD after H₂O₂ or cytokine stimulation.
• Fig. S6. Ser⁷²⁷ is dispensable for the mitoSTAT3-CypD interaction.

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Citation: J. A. Meier, M. Hyun, M. Cantwell, A. Raza, C. Mertens, V. Raje, J. Sisler, E. Tracy, S. Torres-Odio, S. Gispert, P. E. Shaw, H. Baumann, D. Bandyopadhyay, K. Takabe, A. C. Larner, Stress-induced dynamic regulation of mitochondrial STAT3 and its association with cyclophilin D reduce mitochondrial ROS production. Sci. Signal. 10, eaag2588 (2017).

© 2017 American Association for the Advancement of Science