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A protein mutated in Parkinson's disease prevents damage of metabolites and proteins caused by a glycolytic metabolite
Author(s) -
Heremans Isaac P.,
Caligiore Francesco,
Gerin Isabelle,
Bury Marina,
Lutz Marilena,
Graff Julie,
Stroobant Vincent,
Vertommen Didier,
Teleman Aurelio,
Van Schaftingen Emile,
Bommer Guido T.
Publication year - 2022
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2022.36.s1.r5062
Subject(s) - metabolite , glycolysis , enzyme , biochemistry , biology , disease , oxidative stress , parkinson's disease , microbiology and biotechnology , chemistry , medicine
The accumulation of cellular damage is suspected to contribute to aging and neurodegenerative diseases. Oxidative stress and environmental factors likely play a role, but other damaging agents likely remain to be discovered Here we report that an enzyme mutated in hereditary Parkinson’s disease achieves the seemingly impossible task to prevent damage caused by a glycolytic metabolite without affecting the metabolite itself. Inactivation of this enzyme in model systems ranging from flies to human cells leads to the accumulation of a wide range of metabolites and proteins damaged by a newly discovered covalent modification. Thus, this enzyme represents a highly conserved strategy to prevent damage in cells that perform glycolysis. Thereby, it interrupts a fundamental link between carbohydrate metabolism and a type of cellular damage that might contribute to the development of Parkinson’s disease.