Associated Papers
The CaMKII D135N mutation blocks kinase activity and reduces GluN2B binding.
Larsen ME et al.
Biorxiv : the Preprint Server for Biology, 2025
CaMKII monomers are sufficient for GluN2B binding, co-condensation, and synaptic potentiation.
Brown CN et al.
Biorxiv : the Preprint Server for Biology, 2025
GluN2B S1303 phosphorylation by CaMKII or DAPK1: no indication for involvement in ischemia or LTP.
Tullis JE et al.
Iscience, 2021
Glu60 of α-Calcium/calmodulin dependent protein kinase II mediates crosstalk between the regulatory T-site and protein substrate binding region of the active site.
Madhavan M et al.
Archives of Biochemistry and Biophysics, 2020
CaMKII-mediated phosphorylation of GluN2B regulates recombinant NMDA receptor currents in a chloride-dependent manner.
Tavalin SJ et al.
Molecular and Cellular Neurosciences, 2017
Protection of α-CaMKII from Dephosphorylation by GluN2B Subunit of NMDA Receptor Is Abolished by Mutation of Glu96 or His282 of α-CaMKII.
Mayadevi M et al.
Plos One, 2016
Enzymatic activity of CaMKII is not required for its interaction with the glutamate receptor subunit GluN2B.
Barcomb K et al.
Molecular Pharmacology, 2013
Activated CaMKII couples GluN2B and casein kinase 2 to control synaptic NMDA receptors.
Sanz-Clemente A et al.
Cell Reports, 2013
Nucleotides and phosphorylation bi-directionally modulate Ca2+/calmodulin-dependent protein kinase II (CaMKII) binding to the N-methyl-D-aspartate (NMDA) receptor subunit GluN2B.
O'Leary H et al.
The Journal of Biological Chemistry, 2011
Characterization of a central Ca2+/calmodulin-dependent protein kinase IIalpha/beta binding domain in densin that selectively modulates glutamate receptor subunit phosphorylation.
Jiao Y et al.
The Journal of Biological Chemistry, 2011
Phosphorylation status of the NR2B subunit of NMDA receptor regulates its interaction with calcium/calmodulin-dependent protein kinase II.
Raveendran R et al.
Journal of Neurochemistry, 2009
Multivalent interactions of calcium/calmodulin-dependent protein kinase II with the postsynaptic density proteins NR2B, densin-180, and alpha-actinin-2.
Robison AJ et al.
The Journal of Biological Chemistry, 2005
Mechanism and regulation of calcium/calmodulin-dependent protein kinase II targeting to the NR2B subunit of the N-methyl-D-aspartate receptor.
Strack S et al.
The Journal of Biological Chemistry, 2000
Select a paper to view details