Association of Calcium/Calmodulin-dependent Kinase II with Developmentally Regulated Splice Variants of the Postsynaptic Density Protein Densin-180
Open accessAbstract
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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The CaMKII I205K mutation is expected to also disrupt binding to densin-180, α-actinin-2, and other PSD proteins.
“keeping in mind that this mutation is expected to also disrupt the binding to densin-180 and α-actinin-2 (234–236) and other PSD proteins.”
From Synaptic memory and CaMKII (2023) · cites this paper as [234]
The Results and Discussion section shows that CaMKII binds densin-180 variants A, B, and D. It does not examine the CaMKII I205K mutation or show that this mutation disrupts binding to densin-180, α-actinin-2, or other PSD proteins. The residue 205 mentioned there belongs to a densin-180 fragment, not the CaMKII mutation. (LLM, conf=0.85)
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“A third approach takes advantage of a point mutation of CaMKII (I205K), which prevents binding to GluN2B but otherwise reported to function normally (78), keeping in mind that this mutation is expected to also disrupt the binding to densin-180 and a -actinin-2 (234 – 236) and other PSD proteins.”
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- Authors
- Strack, S., Robison, A. J., Bass, M. A., & Colbran, R. J.
- Affiliations
- Vanderbilt University Medical Center (US)
- Corresponding author
- Colbran, Roger J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-08
- Volume
- 275
- Issue
- 33
- Pages
- 25061-25064
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2082845790
- Cited by
- 116
- References
- 0
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 3 · 2022: 2 · 2021: 3 · 2020: 15 · 2019: 3 · 2018: 4 · 2017: 2 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 3 · 2012: 5
- FWCI
- 3.36
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ns037508-04)
- National Cancer Institute (CA68485, P30CA068485)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 20593)
- National Institute of Neurological Disorders and Stroke (NS37508)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- calcium/calmodulin-dependent protein kinase II, postsynaptic density, alternative splicing, CaMKII phosphorylation, synaptic plasticity, NR2B, protein-protein interaction, brain development, membrane targeting
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Brain, Cell Line, Cloning, Molecular, Cytosol, Glutathione Transferase, Kinetics, Microscopy, Fluorescence, Molecular Sequence Data, Phosphorylation, Protein Binding, Recombinant Fusion Proteins, Sialoglycoproteins, Alternative Splicing, Protein Structure, Tertiary, Calcium-Calmodulin-Dependent Protein Kinases, Protein Isoforms, Reverse Transcriptase Polymerase Chain Reaction, Mice, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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