|Detection of GRIN2B/NMDAR2B (Y1252) by Western Blot. Western blot of rat hippocampal lysate showing specific immunolabeling of the approximately 180 kDa NR2B subunit of the NMDAR phosphorylated at Y1252 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: lambda PPase). The blot is identical to the control except that it was incubated in lambda PPase (1200 units for 30 minutes) before being exposed to the Anti-Phospho-NMDA NR2B subunit (Y1252). The immunolabeling is completely eliminated by treatment with lambda PPase.|
NMDA (N-Methyl D-Aspartate) receptors are members of the glutamate receptor family of ligand-gated ion channels. The functional NMDA receptor (NMDAR) is a 650-850 kDa heteromultimer of at least two NR2 (NMDAR2) subunits and two NR1 subunits. NR2 subunits determine overall NMDAR characteristics and mediate NMDAR clustering and synaptic localization through cytoplasmic interaction with PSD-95/SAP90 family members. Upon glutamate binding to NR2, and glycine binding to NR1, the NMDA channel is opened, allowing calcium and sodium influx into the cell. There are four genes that code for NR2 subunits (NR2A-D). The NR2B subunit generates a high conductance NMDAR. Human NR2B (also NR3;GRIN2B and GluR epsilon 2) is a 180-200 kDa, 1458 amino acid (aa), three transmembrane (TM) glycoprotein that contains a 531 aa N-terminal extracellular domain (ECD), and a 646 aa cytoplasmic region. At least three tyrosines are known to be phosphorylated by Fyn in the cytoplasmic region. These include Y1252, Y1336 and Y1472. While much is known about Y1472, little information is available about the consequences of Y1252 and Y1336 phosphorylation.
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