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Originally published In Press as doi:10.1074/jbc.C000319200 on May 25, 2000

J. Biol. Chem., Vol. 275, Issue 33, 25061-25064, August 18, 2000
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ACCELERATED PUBLICATION
Association of Calcium/Calmodulin-dependent Kinase II with Developmentally Regulated Splice Variants of the Postsynaptic Density Protein Densin-180*

Stefan StrackDagger , A. J. Robison§, Martha A. Bass, and Roger J. Colbran

From the Department of Molecular Physiology and Biophysics and Center for Molecular Neuroscience, Vanderbilt University Medical Center, Nashville, Tennessee 37232-0615

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.

* This work was supported by National Institutes (NIH) of Health Grant NS37508 and American Heart Association Grants-in-aid 96010040 (National) and 9950865V (Southeast affiliate). Confocal microscopy was performed using the Vanderbilt Cell Imaging Resource (supported by NIH Grants CA68485 and DK20593).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF266164 (D variant).

Dagger Present address: Dept. of Pharmacology, 2-432 BSB, University of Iowa College of Medicine, Iowa City, IA 52242.

§ Recipient of a Molecular Endocrinology Training Program stipend (5T32DK07563).

To whom correspondence should be addressed: Dept. of Molecular Physiology & Biophysics, Rm. 762, MRB-I, Vanderbilt University, Nashville, TN 37232-0615. Tel.: 615-936-1630; Fax: 615-322-7236; E-mail: Roger.Colbran@mcmail.vanderbilt.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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