BDNF induces transport of PSD-95 to dendrites through PI3K-AKT signaling after NMDA receptor activation

@article{Yoshii2007BDNFIT,
  title={BDNF induces transport of PSD-95 to dendrites through PI3K-AKT signaling after NMDA receptor activation},
  author={Akira Yoshii and Martha Constantine‐Paton},
  journal={Nature Neuroscience},
  year={2007},
  volume={10},
  pages={702-711}
}
The N-methyl-D-aspartate receptor (NMDAR), brain-derived neurotrophic factor (BDNF), postsynaptic density protein 95 (PSD-95) and phosphatidylinositol 3-kinase (PI3K) have all been implicated in long-term potentiation. Here we show that these molecules are involved in a single pathway for synaptic potentiation. In visual cortical neurons in young rodents, the neurotrophin receptor TrkB is associated with PSD-95. When BDNF is applied to cultured visual cortical neurons, PSD-95–labeled synaptic… 
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TrkB and Protein Kinase M ζ Regulate Synaptic Localization of PSD-95 in Developing Cortex
TLDR
This work shows that TrkB and PKMζ, two critical regulators of synaptic plasticity, facilitate PSD-95 targeting to synapses and indicates that palmitoylation can be regulated by a trophic factor, and has implications for neurodevelopmental disorders as well as aging brains.
Protein Kinase Cϵ (PKCϵ) Promotes Synaptogenesis through Membrane Accumulation of the Postsynaptic Density Protein PSD-95*
TLDR
It is shown that the PKCϵ activators dicyclopropanated linoleic acid methyl ester and bryostatin 1 induce phosphorylation of PSD-95 at the serine 295 residue, increase the levels of PSd-95, and enhance its membrane localization, which promotes synaptogenesis.
BDNF-Dependent Recycling Facilitates TrkB Translocation to Postsynaptic Density during LTP via a Rab11-Dependent Pathway
TLDR
It is found that cLTP could stimulate the switch of Rab11 from an inactive to an active form and that GTP-bound Rab11 could enhance the interaction between TrkB-FL and PSD-95, which provides a mechanistic link between Rab11-dependent endocytic recycling and TrkB modulation of synaptic plasticity.
Brain-derived neurotrophic factor (BDNF)-induced mitochondrial motility arrest and presynaptic docking contribute to BDNF-enhanced synaptic transmission.
TLDR
It is found that in cultured hippocampal neurons, application of BDNF for 15 min decreased the percentage of moving mitochondria in axons, a process dependent on the activation of the TrkB receptor and its downstream PI3K and phospholipase-Cγ signaling pathways and the Ca(2+) sensor Miro1 plays an important role in this process.
PSD-95-nNOS Coupling Regulates Contextual Fear Extinction in the Dorsal CA3
TLDR
Because inhibitors of PSD-95-nNOS interaction produce antidepressant and anxiolytic effect without NMDAR-induced side effects, PSD -95- nNOS could be a valuable target for PTSD treatment.
PKC epsilon Promotes Synaptogenesis through Membrane Accumulation of the Postsynaptic Density Protein PSD-95
TLDR
It is shown that the PKCε activators DCPLA-ME and bryostatin 1 induce phosphorylation of PSD-95 at the serine295 residue, increase the levels of PSd-95, and enhance its membrane localization, which indicates thatPKCε promotes synaptogenesis by activating PSD -95 phosphorylated directly, through JNK1 and CaMKII, and also by inducing expression of PS D-95 and synaptophysin.
Postsynaptic BDNF‐TrkB signaling in synapse maturation, plasticity, and disease
TLDR
The current state of understanding BDNF signaling in the context of synaptic development and plasticity is discussed with a focus on the postsynaptic cell and the evidence that basic mechanisms of BDNF function still need to be understood to effectively treat genetic disruptions of these pathways that cause devastating neurodevelopmental diseases is closed.
PSD-95-like membrane associated guanylate kinases (PSD-MAGUKs) and synaptic plasticity
  • Weifeng Xu
  • Biology
    Current Opinion in Neurobiology
  • 2011
BDNF-Induced Increase of PSD-95 in Dendritic Spines Requires Dynamic Microtubule Invasions
TLDR
It is demonstrated in mouse hippocampal neurons that MT entries into spines regulate the increase in postsynaptic density-95 (PSD-95) protein after brain-derived neurotrophic factor (BDNF) treatment, and pharmacological inhibition of MT dynamics abolished the BDNF-induced increase in PSD- 95.
Anchoring and Synaptic stability of PSD-95 is driven by ephrin-B3
TLDR
It is shown using super-resolution imaging, biochemical approaches and in vivo models that the trans-synaptic organizing protein ephrin-B3 controls the synaptic localization and stability of PSD-95 and links these events to changes in neuronal activity via negative regulation of a newly identified mitogen-associated protein kinase (MAPK)-dependent phosphorylation site on ephinus B3, Ser332.
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