[HTML][HTML] Fyn-mediated phosphorylation of NR2B Tyr-1336 controls calpain-mediated NR2B cleavage in neurons and heterologous systems
HY Wu, FC Hsu, AJ Gleichman, I Baconguis… - Journal of Biological …, 2007 - ASBMB
Cleavage of the intracellular carboxyl terminus of the N-methyl-d-aspartate (NMDA) receptor
2 subunit (NR2) by calpain regulates NMDA receptor function and localization. Here, we
show that Fyn-mediated phosphorylation of NR2B controls calpain-mediated NR2B
cleavage. In cultured neurons, calpain-mediated NR2B cleavage is significantly attenuated
by blocking NR2B phosphorylation of Tyr-1336, but not Tyr-1472, via inhibition of Src family
kinase activity or decreasing Fyn levels by small interfering RNA. In HEK cells, mutation of …
2 subunit (NR2) by calpain regulates NMDA receptor function and localization. Here, we
show that Fyn-mediated phosphorylation of NR2B controls calpain-mediated NR2B
cleavage. In cultured neurons, calpain-mediated NR2B cleavage is significantly attenuated
by blocking NR2B phosphorylation of Tyr-1336, but not Tyr-1472, via inhibition of Src family
kinase activity or decreasing Fyn levels by small interfering RNA. In HEK cells, mutation of …