Supplementary Materials

Supplementary Material for:

α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson's disease

Roberto Di Maio, Paul J. Barrett, Eric K. Hoffman, Caitlyn W. Barrett, Alevtina Zharikov, Anupom Borah, Xiaoping Hu, Jennifer McCoy, Charleen T. Chu, Edward A. Burton, Teresa G. Hastings, J. Timothy Greenamyre*

*Corresponding author. Email: jgreena{at}pitt.edu

Published 8 June 2016, Sci. Transl. Med. 8, 342ra78 (2016)
DOI: 10.1126/scitranslmed.aaf3634

This PDF file includes:

  • Materials and Methods
  • Fig. S1. Amounts of α-synuclein and S129-phosphorylated α-synuclein in vivo.
  • Fig. S2. Positive and negative PL interactions with α-synuclein in substantia nigra pars compacta.
  • Fig. S3. Rotenone induces a loss of mitochondrial localization of the nuclear-encoded, imported protein Ndufs3.
  • Fig. S4. All species of α-synuclein used in this study enter cells to an equivalent extent, and when added at 200 nM, they do not change intracellular concentrations of α-synuclein or its localization.
  • Fig. S5. Fibrillar α-synuclein does not affect mitochondrial protein import.
  • Fig. S6. Overexpression of TOM20 and TOM5.
  • Fig. S7. Time course of isolated brain mitochondrial protein import in the absence or presence of monomeric and oligomeric α-synuclein.
  • Fig. S8. Lack of mitochondrial depolarization by α-synuclein during import assays.
  • Fig. S9. Effects of α-synuclein on import and localization of other mitochondrial proteins.
  • Fig. S10. The α-synuclein–TOM20 PL signal colocalizes with mitochondria.
  • Fig. S11. Downstream effects of α-synuclein on mitochondria are blocked by MTS overexpression.
  • Fig. S12. The protective effects of TOM20 overexpression on mitochondrial protein import can be overcome by increased concentrations of α-synuclein.
  • Fig. S13. Structural analysis of the α-synuclein species used in this study.

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