Inactivation of NMDA Receptors by Direct Interaction of Calmodulin with the NR1 Subunit

@article{Ehlers1996InactivationON,
  title={Inactivation of NMDA Receptors by Direct Interaction of Calmodulin with the NR1 Subunit},
  author={Michael D. Ehlers and Su Zhang and Jeffrey Bernhardt and Richard L. Huganir},
  journal={Cell},
  year={1996},
  volume={84},
  pages={745-755}
}
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Calmodulin Mediates Calcium-Dependent Inactivation of N-Methyl-D-Aspartate Receptors
Allosteric changes in the NMDA receptor associated with calcium-dependent inactivation.
Phosphorylation-dependent Regulation ofN-Methyl-d-aspartate Receptors by Calmodulin*
TLDR
It is found that calmodulin interacts with the COOH terminus of the NR1 subunit and inactivates the channels in a Ca2+-dependent manner, and stimulation of metabotropic glutamate receptor 1α, which potentiates NMDA channels through PKC, decreases the ability of NR1 to bind to cal modulin.
Intracellular domains of NR2 alter calcium-dependent inactivation of N-methyl-D-aspartate receptors.
TLDR
The molecular basis for NR2-subunit specificity is examined using chimeric and mutated NMDA receptor subunits expressed in HEK293 cells and it is reported that the intracellular loop immediately distal to the pore-forming P-loop M2 (M2-3 loop), as well as a short region in the C terminus, are involved inNR2- subunit specificity.
Direct Effects of Calmodulin on NMDA Receptor Single-Channel Gating in Rat Hippocampal Granule Cells
TLDR
Calmodulin-dependent inhibition of NMDA receptors will reduce the amplitude and time course of excitatory synaptic currents and thus affect synaptic plasticity and integration of synaptic activity in the CNS.
Competitive binding of α-actinin and calmodulin to the NMDA receptor
The mechanisms by which neurotransmitter receptors are immobilized at postsynaptic sites in neurons are largely unknown. The activity of NMDA (N-methyl-D-aspartate) receptors is mechanosensitive1 and…
PERMEANT ION AND SUBUNIT DEPENDENCE OF EXTERNAL Mg2+ BLOCK OF NMDA RECEPTORS
TLDR
Mg2+ inhibition of whole-cell NMDA currents in cortical neurons, which express NMDA receptors with NR2A or NR2B NR2 subunits, is very sensitive to ionic conditions and can be explained by a kinetic model which incorporates external permeant ion binding sites within the pore.
Interaction with the NMDA receptor locks CaMKII in an active conformation
TLDR
It is shown that regulated CaMKII interaction with two sites on the NMDA receptor subunit NR2B provides a mechanism for the glutamate-induced translocation of the kinase to the synapse in hippocampal neurons.
Intracellular Domains of NR 2 Alter Calcium-Dependent Inactivation of N-Methyl-D-aspartate Receptors
TLDR
The molecular basis for NR2subunit specificity is examined using chimeric and mutated NMDA receptor subunits expressed in HEK293 cells and it is reported that the intracellular loop immediately distal to the pore-forming P-loop M2 (M2–3 loop), as well as a short region in the C terminus, are involved in NR2-sub unit specificity.
Interactions of Calmodulin and α-Actinin with the NR1 Subunit Modulate Ca2+-Dependent Inactivation of NMDA Receptors
TLDR
It is proposed that inactivation can occur after C0 dissociates from α-actinin by two distinct but converging calcium-dependent processes: competitive displacement ofα-act inin by calmodulin and reduction in the affinity of α-Actinin for C0 after binding of calcium to α- actinin.
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Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% ientical in sequence, and these are structurally related, with less than 20% sequence identity, to other excitatory amino acid receptor sub Units.
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