Palmitoylation of superoxide dismutase 1 (SOD1) is increased for familial amyotrophic lateral sclerosis-linked SOD1 mutants

Sarah E. Antinone, Ghanashyam D. Ghadge, Tukiet T. Lam, Lijun Wang, Raymond P. Roos*, William N. Green

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

Background: Mutations in SOD1 cause familial amyotrophic lateral sclerosis (ALS). Results: SOD1 undergoes palmitoylation in the spinal cord and multiple cell types. Palmitoylation occurs predominantly on immature SOD1 and is increased for ALS-linked SOD1 mutants. Conclusion: Palmitoylation is a reversible post-translational modification of SOD1 cysteine residues. Significance: Palmitoylation could affect SOD1 toxicity by altering its folding, membrane targeting, and/or function.

Original languageEnglish (US)
Pages (from-to)21606-21617
Number of pages12
JournalJournal of Biological Chemistry
Volume288
Issue number30
DOIs
StatePublished - Jul 26 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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