Thioredoxin Mediates Oxidation-Dependent Phosphorylation of CRMP2 and Growth Cone Collapse

Akifumi Morinaka, Mayumi Yamada, Rurika Itofusa, Yosuke Funato, Yuta Yoshimura, Fumio Nakamura, Takeshi Yoshimura, Kozo Kaibuchi, Yoshio Goshima, Mikio Hoshino, Hiroyuki Kamiguchi, Hiroaki Miki*

*To whom correspondence should be addressed. E-mail: hmiki{at}protein.osaka-u.ac.jp

This PDF file includes:

• Fig. S1. Immunolocalization of ectopically expressed proteins in growth cones.
• Fig. S2. TRX knockdown does not inhibit serum-induced biochemical changes.
• Fig. S3. Inhibition of the radial migration of cortical neurons by CRMP2 C504S.
• Fig. S4. IAA treatment blocks CRMP2 oligomer formation.
• Fig. S5. RT-PCR analyses of MICAL1 to 3.
• Fig. S6. Rescue of H₂O₂ generation by ectopically expressed MICAL.
• Fig. S7. TRX promotes GSK-3β–dependent CRMP2 phosphorylation in vitro.
• Fig. S8. Sema3A stimulation does not alter the degree of Akt or GSK-3β phosphorylation.
• Fig. S9. Alignment of the amino acid sequence of the region of human CRMP2 containing Cys⁵⁰⁴ with the corresponding sequences.
• Fig. S10. Characterization of the rabbit anti-CRMP2 antibody and the rabbit anti-TRX antibody.

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