| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.52729162 |
| Association between Fyn and NR2A increased immediately after brain ischemia and the increase was maintained for at least 24 h during followed reperfusion , up to about 1 . 7 1 . 8 fold relative to sham groups . 0.52729162^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Thus , whereas application of glutamate to hippocampal slices from control mice increased fyn protein tyrosine kinase ( PTK ) activity more than 2 . 5 fold , these changes were significantly impaired in LP BM 5 MuLV infected mice . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Glutamate activated currents ( evoked every 20 s for up to 20 min ) were increased by src and fyn kinases without affecting the desensitization and deactivation kinetics in NR 1 NR2A but the kinases had no effects in NR 1 NR2B , NR 1 NR2C and NR 1 NR2D receptor channels , suggesting that a phosphorylation site in NR2A is targeted . 4 . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| The SH 3 domain from the Fyn tyrosine kinase possesses a buried hydrogen bond between the side chains of a glutamate ( Glu 24 ) and a serine ( Ser 41 ) residue . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Our data suggest that increased expression of genes encoding the following proteins are involved in oligodendroglial differentiation : Fyn , Erk , p 85 , G alpha 12 guanine nucleotide binding , and transducin beta 2 signal transduction molecules ; glial maturation factor ; the proteasomal subunits C 8 and C 3 ; the proteasomal targeting molecule polyubiquitin ; the cell cycle regulatory proteins Set , protein phosphatase 2A , and nuclear tyrosine phosphatase ( PRL 1 ) ; and the high affinity glutamate cotransporter EAAC 1 . . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Immunoblot analysis revealed that the relative amounts of metabotropic glutamate receptor 1alpha , N ethylmaleimide sensitive fusion protein , protein kinases C , Fyn and TrkB , as well as the neuronal nitric oxide synthase , were significantly higher in seizure developing than in control rats . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Tyrosine phosphorylation of ionotropic glutamate receptors by Fyn or Src differentially modulates their susceptibility to calpain and enhances their binding to spectrin and PSD 95 . ^^^ To test whether and how tyrosine phosphorylation of glutamate ionotropic receptor subunits modulates calpain susceptibility , synaptic membranes were phosphorylated by Fyn or Src , two members of the Src family tyrosine kinases . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Dopamine D 1 dependent trafficking of striatal N methyl D aspartate glutamate receptors requires Fyn protein tyrosine kinase but not DARPP 32 . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NMDA receptor subunits epsilon 1 ( NR2A ) and epsilon 2 ( NR2B ) are substrates for Fyn in the postsynaptic density fraction isolated from the rat brain . ^^^ NMDA receptor subunit epsilon 1 ( NR2A ) was also a substrate for Fyn . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| PSD 95 promotes Fyn mediated tyrosine phosphorylation of the N methyl D aspartate receptor subunit NR2A . ^^^ Results showed that tyrosine phosphorylation of NR2A , one of the NMDA receptor subunits , was reduced in fyn mutant mice . ^^^ NR2A was tyrosine phosphorylated in 293T cells when coexpressed with Fyn . ^^^ Therefore , NR2A would be a substrate for Fyn in vivo . ^^^ Results also showed that PSD 95 , which directly binds to and coclusters with NMDA receptors , promotes Fyn mediated tyrosine phosphorylation of NR2A . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Fyn tyrosine kinase reduces the ethanol inhibition of recombinant NR1 / NR2A but not NR1 / NR2B NMDA receptors expressed in HEK 293 cells . ^^^ In contrast , the inhibition of NR1 / NR2A receptors by ethanol ( 100 mM ) was significantly reduced under conditions of enhanced Fyn mediated tyrosine phosphorylation of the NR2A subunit . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| The ischemia induced increase in the interaction of NR2A and NR2B with the SH 2 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 . . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Using antiphosphotyrosine antibody PY 20 , we find that on expression in HEK cells , 5 Src and Fyn cause detectable tyrosine phosphorylation only of NR2A . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| We have investigated the tyrosine phosphorylation of NMDA receptor subunits NR2A and NR2B by exogenous Src and Fyn and compared this to phosphorylation by tyrosine kinases associated with the postsynaptic density ( PSD ) . ^^^ Src and Fyn phosphorylated similar sites in NR2A and NR2B , tryptic peptide mapping identifying seven and five major tyrosine phosphorylated peptides derived from NR2A and NR2B , respectively . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Activation of Pyk 2 and Src / Fyn kinases led to increased tyrosine phosphorylation of NMDA receptor subunits 2A and B ( NR2A / B ) and was blocked by a selective mGluR 1 antagonist , 7 ( hydroxyamino ) cyclopropa [ b ] chromen 1a carboxylate ethyl ester , but not an mGluR 5 antagonist , 2 methyl 6 ( phenylethynyl ) pyridine . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| We have shown that an Src family kinase Fyn phosphorylates NR2A and NR2B subunits of the NMDA receptor . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| In this study , we investigated the effects of protein tyrosine kinase ( PTK ) and protein tyrosine phosphatase ( PTP ) on the tyrosine phosphorylation of N methyl D aspartate receptor subunit 2A ( NR2A ) and the interactions among NR2A , postsynaptic density protein 95 ( PSD 95 ) , Fyn / Src after brain ischemia / reperfusion ( I / R ) . ^^^ The following results were observed : ( 1 ) the increase in tyrosine phosphorylation of NR2A induced by I / R was suppressed by genistein , an inhibitor of PTK , but was further enhanced by sodium orthovanadate , an inhibitor of PTP , which were administered to the SD rats 20 min before ischemia . ( 2 ) Importantly , genistein and sodium orthovanadate increased and decreased the interactions involving NR2A , PSD 95 , Fyn and Src , respectively . ^^^ These results demonstrated that PTK and PTP were involved in regulating tyrosine phosphorylation of NR2A through changing the interaction among NR2A , PSD 95 , Fyn / Src . . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Spatial learning induced phosphorylation of TrkB , Fyn , and NR2B , but not NR2A , in the hippocampus . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Suppression of postsynaptic density protein 95 expression attenuates increased tyrosine phosphorylation of NR2A subunits of N methyl D aspartate receptors and interactions of Src and Fyn with NR2A after transient brain ischemia in rat hippocampus . ^^^ The effects of suppression of postsynaptic density protein 95 ( PSD 95 ) expression on the increased tyrosine phosphorylation of N methyl D aspartate receptor subunit NR2A and interactions of Src and Fyn with NR2A after brain ischemia were investigated by immunoprecipitation and immunoblotting . ^^^ Intracerebroventricular infusion of PSD 95 antisense oligonucleotides ( every 24 h for 3 days before ischemia ) , but not missense oligonucleotides or vehicle , not only markedly decreased the protein level of PSD 95 but also attenuated the elevated tyrosine phosphorylation of NR2A and interactions of Src and Fyn with NR2A induced by 6 h of reperfusion following ischemia in the hippocampus . ^^^ The protein levels of NR2A , Src and Fyn had no differences under the above conditions . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Since brain ischemia results in NMDA receptor over excitation and Src family protein tyrosine kinase mediated tyrosine phosphorylation of NMDA receptor subunit 2A ( NR2A ) enhances NMDA receptor activity , we examined the effects of lithium on tyrosine phosphorylation of NR2A and its interactions with Src and Fyn ( two members of the Src family of protein tyrosine kinases ) mediated by PSD 95 ( postsynaptic density protein 95 kDa ) after 6 h of reperfusion following 15 min of ischemia ( I / R ) , which was induced by occlusion of the four vessels in Sprague Dawley rats . ^^^ After abdominal injection of LiCl ( 2 mg / kg ) for 7 days , the data showed that together with the significant decrease in I / R induced tyrosine phosphorylation of NR2A , the interactions of NR2A with Src and Fyn mediated by PSD 95 were also decreased significantly . ^^^ However , lithium pretreatment did not alter the total protein levels of NR2A , Src , Fyn and PSD 95 . ^^^ These results suggest that the inhibition of NR2A tyrosine phosphorylation and its interactions with Src and Fyn mediated by PSD 95 may contribute to the lithium induced downregulation of NMDA receptor function and provide neuroprotection against excitotoxicity . . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| Tyrosine phosphorylation of the NMDA receptor subunit NR2A by Src or Fyn has been implicated in the up regulation of NMDA receptor activity . ^^^ In order to investigate the possible mechanism of the neuroprotective action of SY 21 , we examined the effects of SY 21 on the ischemia / reperfusion induced increases in tyrosine phosphorylation of the NMDA receptor subunit 2A ( NR2A ) and on the interactions involving NR2A , PSD 95 and Src / Fyn . ^^^ Also , SY 21 attenuated the increased interactions involving NR2A , PSD 95 , Fyn and Src . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| We also found that the increase in NR2A and NR2B proteins in heterozygous reeler was dependent on Fyn , because this change was absent in heterozygous reeler / homozygous Fyn deficient double mutant mice . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| In the first presentation , Dorit Ron presented data showing how activation of Fyn or Src tyrosine kinases differentially regulated the cell surface expression and activity of NR2A and NR2B containing NMDA receptors . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| In a human embryonic kidney ( HEK ) 293 cell expression system , PTPalpha enhanced fyn mediated NR2A and NR2B tyrosine phosphorylation by several fold . ^^^ |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q12879 and P06241 |
Pubmed |
SVM Score :0.0 |
| NA |
|