Supplementary Materials for:

ROMO1 Is an Essential Redox-Dependent Regulator of Mitochondrial Dynamics

Matthew Norton, Andy Cheuk-Him Ng, Stephen Baird, Ariane Dumoulin, Timothy Shutt, Nancy Mah, Miguel A. Andrade-Navarro, Heidi M. McBride, Robert A. Screaton*

*Corresponding author. E-mail: rob@arc.cheo.ca

This PDF file includes:

• Fig. S1. The high-throughput mitochondrial morphology screen identifies ROMO1 as a regulator of mitochondrial fusion.
• Fig. S2. Full-length multiple-sequence alignment of ROMO1 with orthologs.
• Fig. S3. Reversible oxidation of ROMO1 and rescue of mitochondrial morphology with siRNA-resistant ROMO1 constructs.
• Fig. S4. ROMO1 associates with, but does not affect, integrity of MINOS.
• Fig. S5. Normal cellular ATP content and mitochondrial membrane potential in ROMO1 knockdown cells.
• Fig. S6. Effect of ROMO1 status on OPA1 isoform balance.
• References (66, 67)

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Citation: M. Norton, A. C.-H. Ng, S. Baird, A. Dumoulin, T. Shutt, N. Mah, M. A. Andrade-Navarro, H. M. McBride, R. A. Screaton, ROMO1 Is an Essential Redox-Dependent Regulator of Mitochondrial Dynamics. Sci. Signal. 7, ra10 (2014).

© 2014 American Association for the Advancement of Science