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Fructose 1,6-Bisphosphatase 2 Plays a Crucial Role in the Induction and Maintenance of Long-Term Potentiation
- Source :
- Cells, Volume 9, Issue 6, Cells, Vol 9, Iss 1375, p 1375 (2020)
- Publication Year :
- 2020
- Publisher :
- MDPI, 2020.
-
Abstract
- Long-term potentiation (LTP) is a molecular basis of memory formation. Here, we demonstrate that LTP critically depends on fructose 1,6-bisphosphatase 2 (Fbp2)&mdash<br />a glyconeogenic enzyme and moonlighting protein protecting mitochondria against stress. We show that LTP induction regulates Fbp2 association with neuronal mitochondria and Camk2 and that the Fbp2&ndash<br />Camk2 interaction correlates with Camk2 autophosphorylation. Silencing of Fbp2 expression or simultaneous inhibition and tetramerization of the enzyme with a synthetic effector mimicking the action of physiological inhibitors (NAD+ and AMP) abolishes Camk2 autoactivation and blocks formation of the early phase of LTP and expression of the late phase LTP markers. Astrocyte-derived lactate reduces NAD+/NADH ratio in neurons and thus diminishes the pool of tetrameric and increases the fraction of dimeric Fbp2. We therefore hypothesize that this NAD+-level-dependent increase of the Fbp2 dimer/tetramer ratio might be a crucial mechanism in which astrocyte&ndash<br />neuron lactate shuttle stimulates LTP formation.
- Subjects :
- Protein moonlighting
memory formation
Long-Term Potentiation
Fructose 1,6-bisphosphatase
Mitochondrion
Hippocampus
Article
LTP induction
Animals
Gene Silencing
lcsh:QH301-705.5
Cells, Cultured
Membrane Potential, Mitochondrial
Neurons
biology
Effector
Chemistry
musculoskeletal, neural, and ocular physiology
Autophosphorylation
Long-term potentiation
General Medicine
Cell biology
Fructose-Bisphosphatase
Mitochondria
Mice, Inbred C57BL
Protein Transport
protein–protein interaction
lcsh:Biology (General)
nervous system
Animals, Newborn
Synapses
biology.protein
moonlighting protein
Calcium
NAD+ kinase
Calcium-Calmodulin-Dependent Protein Kinase Type 2
astrocyte-neuron lactate shuttle
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 20734409
- Volume :
- 9
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Cells
- Accession number :
- edsair.doi.dedup.....dc396a18d4d7d1447a10bf4df83a3a2d