Enzymatic activity of CaMKII is not required for its interaction with the glutamate receptor subunit GluN2B.

ABSTRACT: Binding of the Ca²⁺/calmodulin (CaM)-dependent protein kinase II (CaMKII) to the NMDA-type glutamate receptor subunit GluN2B is an important control mechanism for the regulation of synaptic strength. CaMKII binding to GluN2B and CaMKII translocation to synapses are induced by an initial Ca²⁺/CaM stimulus, which also activates the kinase. Indeed, several mechanistically different CaMKII inhibitors [tatCN21 and KN-93 (N-[2-[[[3-(4-chlorophenyl)-2-propenyl]methylamino]methyl]phenyl]-N-(2-hydroxyethyl)-4-methoxybenzenesulphonamide)] and inactivating mutations (K42M, A302R, and T305/T306D) impair this interaction, suggesting that it requires CaMKII enzymatic activity. However, this study shows that two general kinase inhibitors, H7 [1-(5-isoquinolinylsulfonyl)-2-methylpiperazine] and staurospor

SUBMITTER: Barcomb K 

PROVIDER: S-EPMC3834147 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature