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• W3157848824 endingPage "4800" @default.
• W3157848824 startingPage "4800" @default.
• W3157848824 abstract "Fructose 1,6-bisphosphatase 2 (Fbp2) is a gluconeogenic enzyme and multifunctional protein modulating mitochondrial function and synaptic plasticity via protein-protein interactions. The ability of Fbp2 to bind to its cellular partners depends on a quaternary arrangement of the protein. NAD+ and AMP stabilize an inactive T-state of Fbp2 and thus, affect these interactions. However, more subtle structural changes evoked by the binding of catalytic cations may also change the affinity of Fbp2 to its cellular partners. In this report, we demonstrate that Fbp2 interacts with Co2+, a cation which in excessive concentrations, causes pathologies of the central nervous system and which has been shown to provoke the octal-like events in hippocampal slices. We describe for the first time the kinetics of Fbp2 in the presence of Co2+, and we provide a line of evidence that Co2+ blocks the AMP-induced transition of Fbp2 to the canonical T-state triggering instead of a new, non-canonical T-state. In such a state, Fbp2 is still partially active and may interact with its binding partners e.g., Ca2+/calmodulin-dependent protein kinase 2α (Camk2α). The Fbp2-Camk2α complex seems to be restricted to mitochondria membrane and it facilitates the Camk2α autoactivation and thus, synaptic plasticity." @default.
• W3157848824 created "2021-05-10" @default.
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• W3157848824 date "2021-04-30" @default.
• W3157848824 modified "2023-09-26" @default.
• W3157848824 title "Cobalt Regulates Activation of Camk2α in Neurons by Influencing Fructose 1,6-Bisphosphatase 2 Quaternary Structure and Subcellular Localization" @default.
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• W3157848824 doi "https://doi.org/10.3390/ijms22094800" @default.
• W3157848824 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8125063" @default.
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• W3157848824 hasPublicationYear "2021" @default.
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