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

Andre Laval Samson, Anja Sylvia Knaupp, Itamar Kass, Oded Kleifeld, Emilia Maria Marijanovic, Victoria Anne Hughes, Christopher Joseph Lupton, Ashley Maurice Buckle, Stephen Paul Bottomley, Robert Lindsay Medcalf

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28 Citations (Scopus)

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
Publication statusPublished - 2014

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