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Association of Calcium/Calmodulin-dependent Kinase II with Developmentally Regulated Splice Variants of the Postsynaptic Density Protein Densin-180
Journal article   Open access   Peer reviewed

Association of Calcium/Calmodulin-dependent Kinase II with Developmentally Regulated Splice Variants of the Postsynaptic Density Protein Densin-180

Stefan Strack, A. J Robison, Martha A Bass and Roger J Colbran
The Journal of biological chemistry, Vol.275(33), pp.25061-25064
08/18/2000
DOI: 10.1074/jbc.C000319200
PMID: 10827168
url
https://doi.org/10.1074/jbc.C000319200View
Published (Version of record) Open Access

Abstract

In a continuing search for proteins that target calcium/calmodulin-dependent protein kinase II (CaMKII) to postsynaptic density (PSD) substrates important in synaptic plasticity, we showed that the PSD protein densin-180 binds CaMKII. Four putative splice variants (A-D) of the cytosolic tail of densin-180 are shown to be differentially expressed during brain development. Densin-180 splicing affects CaMKII phosphorylation of specific serine residues. Variants A, B, and D, but not C, bind CaMKII stoichiometrically and with high affinity, mediated by a differentially spliced domain. Densin-180 differs from the previously identified CaMKII-binding protein NR2B in that binding does not strictly require CaMKII autophosphorylation. Binding of densin-180 and NR2B to CaMKII is noncompetitive, indicating different interaction sites on CaMKII. Expression of the membrane-targeted CaMKII-binding domain of densin-180 confers membrane localization to coexpressed CaMKII without requiring calcium mobilization, suggesting that densin-180 plays a role in the constitutive association of CaMKII with PSDs.

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