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

doi:10.1074/jbc.M113.487231

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

Microbiology-Immunology

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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 language	English (US)
Pages (from-to)	21606-21617
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	288
Issue number	30
DOIs	https://doi.org/10.1074/jbc.M113.487231
State	Published - Jul 26 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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

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.",

author = "Antinone, {Sarah E.} and Ghadge, {Ghanashyam D.} and Lam, {Tukiet T.} and Lijun Wang and Roos, {Raymond P.} and Green, {William N.}",

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Palmitoylation of superoxide dismutase 1 (SOD1) is increased for familial amyotrophic lateral sclerosis-linked SOD1 mutants. / Antinone, Sarah E.; Ghadge, Ghanashyam D.; Lam, Tukiet T.; Wang, Lijun; Roos, Raymond P.; Green, William N.

In: Journal of Biological Chemistry, Vol. 288, No. 30, 26.07.2013, p. 21606-21617.

Research output: Contribution to journal › Article › peer-review

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T1 - Palmitoylation of superoxide dismutase 1 (SOD1) is increased for familial amyotrophic lateral sclerosis-linked SOD1 mutants

AU - Antinone, Sarah E.

AU - Ghadge, Ghanashyam D.

AU - Lam, Tukiet T.

AU - Wang, Lijun

AU - Roos, Raymond P.

AU - Green, William N.

PY - 2013/7/26

Y1 - 2013/7/26

N2 - 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.

AB - 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.

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

Abstract

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