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
View on AAAS
ncbi.nlm.nih.gov
605 Citations
Highly Influential Citations
13
Background Citations
168
Methods Citations
13
Results Citations
5

605 Citations

Citation Type

Citation Type

G-protein-coupled receptors act via protein kinase C and Src to regulate NMDA receptors
  • 361
Src kinases: a hub for NMDA receptor regulation
  • 702
NMDA receptor regulation by Src kinase signalling in excitatory synaptic transmission and plasticity
  • 282
Regulation of NMDA receptors by cyclin-dependent kinase-5
  • B. Li, M. Sun, +6 authors H. Pant
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2001
  • 256
  • PDF
Src, N-methyl-D-aspartate (NMDA) receptors, and synaptic plasticity.
  • M. Salter
  • Chemistry, Medicine
  • Biochemical pharmacology
  • 1998
  • 112
NMDA receptor function is regulated by the inhibitory scaffolding protein, RACK1
  • 188
  • PDF
Tyrosine kinase potentiates NMDA receptor currents by reducing tonic zinc inhibition
  • 184
Post-synaptic density-93 mediates tyrosine-phosphorylation of the N-methyl-d-aspartate receptors
  • 38
Src, a molecular switch governing gain control of synaptic transmission mediated by N-methyl-D-aspartate receptors.
  • X. Yu, M. Salter
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1999
  • 114
  • PDF
Modulation of NMDA receptors.
  • 24
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 29 REFERENCES
Regulation of NMDA receptors by tyrosine kinases and phosphatases
  • 677
Inactivation of NMDA Receptors by Direct Interaction of Calmodulin with the NR1 Subunit
  • 520
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
  • 134
  • PDF
Differential Tyrosine Phosphorylation of N-Methyl-D-aspartate Receptor Subunits (*)
  • 282
  • PDF
Subtype‐specific regulation of recombinant NMDA receptor‐channels by protein tyrosine kinases of the src family.
  • 318
Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
  • 1,820
Regulation of NMDA channel function by endogenous Ca2+-dependent phosphatase
  • 480
Protein kinase C reduces Mg2+ block of NMDA-receptor channels as a mechanism of modulation
  • 930
Phosphorylation of amino acid neurotransmitter receptors in synaptic plasticity
  • 225
The major tyrosine-phosphorylated protein in the postsynaptic density fraction is N-methyl-D-aspartate receptor subunit 2B.
  • 303
  • PDF
...
1
2
3
...