Fyn phosphorylates Nmdar2b

Stable Identifier
R-MMU-3928613
Type
Reaction [transition]
Species
Mus musculus
Compartment
General
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Fyn phosphorylates Nmdar2b

Protein phosphorylation is an important mechanism modulating the function of NMDA receptors (NMDARs). SRC-family kinases that associate with EPHB are important for the phosphorylation of ionotropic glutamate receptor, NR2B (NMDAR2B, GRIN2B) Tyrosines 1252, 1336, and 1474 (1252, 1336, and 1472 in mouse) on NR2B are phosphorylated by FYN/SRC bound to EPHB2, thereby enhancing NMDA-dependent calcium influx upon glutamate stimulation (Takasu et al. 2002, Dalva et al. 2000). Tyrosine phosphorylation of NMDAR2B also regulates the surface expression of NMDARs. EPHB mediated phosphorylation of NMDARs can also increase the surface retention of NMDAR2B-containing NMDARs by preventing clathrin-dependent endocytosis. Phosphorylation at tyrosine 1474 (mouse Y1472) of NMDAR2B blocks binding of the mu2 subunit of clathrin adaptor protein 2 (AP2) complex thus preventing clathrin-dependent endocytosis (Chen & Roche 2007).

Literature References
PubMed ID Title Journal Year
11136979 EphB receptors interact with NMDA receptors and regulate excitatory synapse formation

Dalva, MB, Takasu, MA, Lin, MZ, Shamah, SM, Hu, L, Gale, NW, Greenberg, ME

Cell 2000
11799243 Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors

Takasu, MA, Dalva, MB, Zigmond, RE, Greenberg, ME

Science 2002
Participants
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of ephrin-B2:Ephb2:Fyn:Nmdar [plasma membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
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