Glutathionylation primes soluble glyceraldehyde-3-phosphate dehydrogenase for late collapse into insoluble aggregates

Protein aggregation is a complex physiological process, primarily determined by stress-related factors revealing the hidden aggregation propensity of proteins that otherwise are fully soluble. Here we report a mechanism by which glycolytic glyceraldehyde-3-phosphate dehydrogenase of Arabidopsis thal...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2019-12, Vol.116 (51), p.26057-26065
Hauptverfasser:	Zaffagnini, Mirko, Marchand, Christophe H., Malferrari, Marco, Murail, Samuel, Bonacchi, Sara, Genovese, Damiano, Montalti, Marco, Venturoli, Giovanni, Falini, Giuseppe, Baaden, Marc, Lemaire, Stéphane D., Fermani, Simona, Trost, Paolo
Format:	Artikel
Sprache:	eng
Schlagworte:	Agglomeration Aggregates Arabidopsis - metabolism Arabidopsis Proteins - chemistry Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Biological Sciences Catalytic Domain Chain branching Collapse Dehydrogenase Dehydrogenases Glutaredoxins - metabolism Glutathione Glutathione - chemistry Glutathione - metabolism Glutathione Disulfide - chemistry Glyceraldehyde-3-phosphate dehydrogenase Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) - chemistry Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) - genetics Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) - metabolism Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry Glyceraldehyde-3-Phosphate Dehydrogenases - genetics Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism Glycolysis Kinetics Lag phase Molecular Dynamics Simulation Molecular Sequence Annotation Oxidation-Reduction Physiological effects Physiology Protein Folding Protein interaction Proteins Reductases Solubility Thioredoxins - metabolism
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