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}
}

Figures from this paper

Phosphorylation-dependent Regulation ofN-Methyl-d-aspartate Receptors by Calmodulin*
TLDR
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TLDR
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TLDR
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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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