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Disulfide bridge formation prevents CaMKII/Calmodulin interaction in Parkinson's disease

Di Maio, R.; General, I. J.; Furbee, E.; Ayoobc, J. C.; Castro, S. L.; Bahar, I.; Greenamyre, J. T.; Pullara, F.

2020-02-15 neuroscience
10.1101/2020.02.14.947960 bioRxiv
Show abstract

There is increasing evidence for disordered Ca2+ signaling in dopamine neurons in Parkinsons disease (PD), and this likely involves altered Ca2+/calmodulin-dependent protein kinase II (CaMKII) function. Previous work suggests that oxidative stress - a major feature in PD pathogenesis - affects regulatory methionine residues that sustain CaMKII activity in a Ca2+/CaM-independent manner. Here, applying computational modeling, we predicted formation of a defined disulfide bridge close to the CaMKII docking site for Ca2+/CaM binding. In vitro and in vivo investigations using PD models revealed formation of a disulfide bridge and loss of the CaMKII-calmodulin interaction. Mutagenesis of the relevant cysteine residues abrogated disulfide bridge formation and recovered the CaMKII-calmodulin interaction. Importantly, dopamine neurons from post-mortem PD brain specimens also lost this regulatory protein-protein interaction, providing relevance in the human disease. This study provides novel insights into oxidative CaMKII-CaM dysfunction, which may contribute to the pathophysiology of PD.

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