Title : Phosphorylation of Tyrosine 1070 at the GluN2B Subunit Is Regulated by Synaptic Activity and Critical for Surface Expression of N-Methyl-D-aspartate (NMDA) Receptors.

Pub. Date : 2015 Sep 18

PMID : 26229100






5 Functional Relationships(s)
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1 In this study we identified a tyrosine site on the GluN2B subunit, Tyr-1070, which was phosphorylated by a proto-oncogene tyrosine-protein (Fyn) kinase and critical for the surface expression of GluN2B-containing NMDARs. Tyrosine FYN proto-oncogene, Src family tyrosine kinase Homo sapiens
2 In this study we identified a tyrosine site on the GluN2B subunit, Tyr-1070, which was phosphorylated by a proto-oncogene tyrosine-protein (Fyn) kinase and critical for the surface expression of GluN2B-containing NMDARs. Tyrosine FYN proto-oncogene, Src family tyrosine kinase Homo sapiens
3 The phosphorylation of GluN2B at Tyr-1070 was required for binding of Fyn kinase to GluN2B, which up-regulated the phosphorylation of GluN2B at Tyr-1472. Tyrosine FYN proto-oncogene, Src family tyrosine kinase Homo sapiens
4 The phosphorylation of GluN2B at Tyr-1070 was required for binding of Fyn kinase to GluN2B, which up-regulated the phosphorylation of GluN2B at Tyr-1472. Tyrosine FYN proto-oncogene, Src family tyrosine kinase Homo sapiens
5 Moreover, our results revealed that the phosphorylation change of GluN2B at Tyr-1070 accompanied the Tyr-1472 phosphorylation and Fyn associated with GluN2B in synaptic plasticity induced by both chemical and contextual fear learning. Tyrosine FYN proto-oncogene, Src family tyrosine kinase Homo sapiens