NMDA Channel Regulation by Channel-Associated Protein Tyrosine Kinase Src

@article{Yu1997NMDACR,
  title={NMDA Channel Regulation by Channel-Associated Protein Tyrosine Kinase Src},
  author={X. Yu and R. Askalan and G. Keil and M. Salter},
  journal={Science},
  year={1997},
  volume={275},
  pages={674 - 678}
}
The N-methyl-D-aspartate (NMDA) receptor mediates synaptic transmission and plasticity in the central nervous system (CNS) and is regulated by tyrosine phosphorylation. In membrane patches excised from mammalian central neurons, the endogenous tyrosine kinase Src was shown to regulate the activity of NMDA channels. The action of Src required a sequence [Src(40–58)] within the noncatalytic, unique domain of Src. In addition, Src coprecipitated with NMDA receptor proteins. Finally, endogenous Src… Expand
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  • Chemistry, Medicine
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  • 1998
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Src, a molecular switch governing gain control of synaptic transmission mediated by N-methyl-D-aspartate receptors.
  • X. Yu, M. Salter
  • Biology, Medicine
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  • 1999
Modulation of NMDA receptors.
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References

SHOWING 1-10 OF 29 REFERENCES
Regulation of NMDA receptors by tyrosine kinases and phosphatases
Inactivation of NMDA Receptors by Direct Interaction of Calmodulin with the NR1 Subunit
Ca(2+)-independent reduction of N-methyl-D-aspartate channel activity by protein tyrosine phosphatase.
  • Y. Wang, X. Yu, M. Salter
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1996
Differential Tyrosine Phosphorylation of N-Methyl-D-aspartate Receptor Subunits (*)
Subtype‐specific regulation of recombinant NMDA receptor‐channels by protein tyrosine kinases of the src family.
Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
Regulation of NMDA channel function by endogenous Ca2+-dependent phosphatase
Protein kinase C reduces Mg2+ block of NMDA-receptor channels as a mechanism of modulation
Phosphorylation of amino acid neurotransmitter receptors in synaptic plasticity
The major tyrosine-phosphorylated protein in the postsynaptic density fraction is N-methyl-D-aspartate receptor subunit 2B.
...
1
2
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