NMDA receptor activation results in tyrosine phosphorylation of NMDA receptor subunit 2A(NR2A) and interaction of Pyk2 and Src with NR2A after transient cerebral ischemia and reperfusion

  title={NMDA receptor activation results in tyrosine phosphorylation of NMDA receptor subunit 2A(NR2A) and interaction of Pyk2 and Src with NR2A after transient cerebral ischemia and reperfusion},
  author={Yong Liu and Guangyi Zhang and Can Gao and Xiao-Yu Hou},
  journal={Brain Research},

S-nitrosylation of c-Src via NMDAR-nNOS module promotes c-Src activation and NR2A phosphorylation in cerebral ischemia/reperfusion

The results show that S-nitrosylation and the phosphorylation of c-Src were induced after cerebral I/R in rats, and administration of nN OS inhibitor 7-NI, nNOS antisense oligonucleotides and exogenous NO donor sodium nitroprusside diminished the increased S- Nitrosylated and phosphorylated of c -Src during cerebral I-R.



Mechanisms of regulation of tyrosine phosphorylation of NMDA receptor subunit 2B after cerebral ischemia/reperfusion.

The increase of the tyrosine phosphorylation of NR2B induced by I/R has relation to NR and L-type VGCC; PTK and PTP participate in the regulation of the autoreperfusion ofNR2B during I/ R.

The Effect of Transient Global Ischemia on the Interaction of Src and Fyn with the N-Methyl-d-Aspartate Receptor and Postsynaptic Densities: Possible Involvement of Src Homology 2 Domains

The ischemia-induced increase in the interaction of NR2A and NR2B with the SH2 domains of Src and Fyn suggests a possible mechanism for the recruitment of signaling proteins to the PSD and may contribute to altered signal transduction in the postischemic hippocampus.

Altered Association of Protein Tyrosine Kinases with Postsynaptic Densities after Transient Cerebral Ischemia in the Rat Brain

The results demonstrate that ischemia results in selective changes in the association of protein tyrosine kinases with the PSD which may account for ischemic-induced increases in the tyosine phosphorylation of PSD proteins.

Differential Regulation of Proline-rich Tyrosine Kinase 2/Cell Adhesion Kinase β (PYK2/CAKβ) and pp125FAK by Glutamate and Depolarization in Rat Hippocampus*

In hippocampal slices, tyrosine phosphorylation of pp125FAK and PYK2/CAKβ are regulated differentially by pathways involving Ca2+ and protein kinase C, which may be important for neuronal survival, and synaptic plasticity.

Characterization of Protein Kinase A and Protein Kinase C Phosphorylation of the N-Methyl-D-aspartate Receptor NR1 Subunit Using Phosphorylation Site-specific Antibodies*

It is demonstrated that PKA and PKC phosphorylate distinct residues within a small region of the NR1 sub unit and differentially affect the subcellular distribution of theNR1 subunit.

Differential Tyrosine Phosphorylation of N-Methyl-D-aspartate Receptor Subunits (*)

Immunocytochemical staining with an anti-phosphotyrosine antibody demonstrates that there are high levels of phosphotYrosine, which co-localizes with glutamate receptors at excitatory synapses on cultured hippocampal neurons and suggests that tyrosine phosphorylation of the NR2 subunits may be important for regulating NMDA receptor function.

Protein Tyrosine Kinase‐Mediated Potentiation of Currents from Cloned NMDA Receptors

It appears that tyrosine residues responsible for potentiation are continually rephosphorylated by some long‐term PTK activity that was induced via insulin treatment.

NMDA Channel Regulation by Channel-Associated Protein Tyrosine Kinase Src

In membrane patches excised from mammalian central neurons, the endogenous tyrosine kinase Src was shown to regulate the activity of NMDA channels and coprecipitated with NMDA receptor proteins.

A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation

It is proposed that Pyk2 acts with Src to link Gi- and Gq-coupled receptors with Grb2 and Sos to activate the MAP kinase signalling pathway in PC12 cells.

Activation of Protein-tyrosine Kinase Pyk2 Is Downstream of Syk in FcεRI Signaling*

It is reported that Pyk2, another member of the focal adhesion kinase family, was present in the RBL-2H3 mast cell line and was rapidly tyrosine-phosphorylated and activated after FcεRI aggregation and may play a role in cell secretion.