Oxidation of an exposed methionine instigates the aggregation of glyceraldehyde-3-phosphate dehydrogenase

Andre L. Samson, Anja S. Knaupp, Itamar Kass, Oded Kleifeld, Emilia M. Marijanovic, Victoria A. Hughes, Chris J. Lupton, Ashley M. Buckle, Stephen P. Bottomley, Robert L. Medcalf

Research output: Contribution to journalArticlepeer-review

Abstract

Background: GAPDH is a glycolytic enzyme that aggregates during disease. Cysteine oxidation is the putative cause of aggregation. Whether GAPDH aggregation influences disease is unknown.

Results: Mutating Met-46 renders GAPDH resistant to free radical-induced aggregation.

Conclusion: Methionine oxidation, rather than cysteine oxidation, is a primary event that instigates GAPDH aggregation.

Significance: Mutating Met-46 in vivo should elucidate whether GAPDH aggregation causally contributes to disease.

Original languageEnglish
Pages (from-to)26922-26936
Number of pages15
JournalJournal of Biological Chemistry
Volume289
Issue number39
DOIs
StatePublished - 26 Sep 2014
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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