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Novel Anchorage of GluR2/3 to the Postsynaptic Density by the AMPA Receptor–Binding Protein ABP
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PICK1 Targets Activated Protein Kinase Cα to AMPA Receptor Clusters in Spines of Hippocampal Neurons and Reduces Surface Levels of the AMPA-Type Glutamate Receptor Subunit 2
TLDR
It is indicated that PICK1 functions as a targeting and transport protein that directs the activated form of PKCα to GluR2 in spines, leading to the activity-dependent release of GLUR2 from synaptic anchor proteins and the P Pick1-dependent transport of Glu R2 from the synaptic membrane.
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RNA Editing at Arg607 Controls AMPA Receptor Exit from the Endoplasmic Reticulum
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Mutagenesis Reveals a Role for ABP/GRIP Binding to GluR2 in Synaptic Surface Accumulation of the AMPA Receptor
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Biphasic Coupling of Neuronal Nitric Oxide Synthase Phosphorylation to the NMDA Receptor Regulates AMPA Receptor Trafficking and Neuronal Cell Death
TLDR
A swinging domain model for the regulation of nNOS is proposed: S1412 phosphorylation facilitates electron flow within the reductase module ofnNOS, increasing nN OS sensitivity to Ca2+-calmodulin.
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The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs.
In this study, we demonstrate specific interaction of the GluR2 alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptor subunit C-terminal peptide with an ATPase…
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A GluR1-cGKII Interaction Regulates AMPA Receptor Trafficking
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NSF ATPase and α-/β-SNAPs Disassemble the AMPA Receptor-PICK1 Complex
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NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA receptor-PICK1 complex.
TLDR
This work shows that GluR2, PICK1, NSF, and alpha-/beta-SNAPs form a complex in the presence of ATPgammaS and reports a non-SNARE substrate for NSF disassembly activity, demonstrating that the previously reported synaptic stabilization of AMPARs by NSF involves disruption of GLUR2-PICK1 interactions.
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Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons
TLDR
It is shown that a newly identified component of rat postsynaptic densities (PSDs), AIDA-1d, can regulate global protein synthesis by altering nucleolar numbers by regulating nucleolar assembly.
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