Calcium/calmodulin-dependent protein kinase II inhibitor protein: localization of isoforms in rat brain
Abstract
A second isoform of Ca2+/calmodulin-dependent-kinase II inhibitor protein (CaM-KIIN) has been identified using the yeast two-hybrid screen. The 1.8kb message encodes a 78 residue CaM-KIINalpha that is 65% identical in its putative open-reading frame and 95% identical in its inhibitory domain to the previously characterized CaM-KIINbeta. CaM-KIINalpha exhibits inhibitory properties towards recombinant mouse CaM-kinase IIalpha indistinguishable from CaM-KIINbeta. The 27 amino acid inhibitory peptide (CaM-KIINtide) derived from CaM-KIIN has the ability to inhibit brain CaM-kinase II activity from multiple organisms including rat, Drosophila and goldfish. Northern analysis of various rat tissues indicates that CaM-KIINalpha is specific to brain whereas CaM-KIINbeta message is also present in testis. In situ hybridization shows a general distribution of both isoforms in rat brain with stronger localization of CaM-KIINbeta in cerebellum and hindbrain and CaM-KIINalpha in frontal cortex, hippocampus and inferior colliculus. An antibody that recognizes both isoforms shows a distribution of CaM-KIIN in rat brain that correlates with immunoreactivity of CaM-kinase II. In cultured mature hippocampal neurons, CaM-KIIN is present in cell bodies and dendrites but, unlike CaM-kinase II, does not display punctate staining at synapses. These results suggest a localized function for CaM-KIIN in inhibiting specialized pools of CaM-kinase II.
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CaMKIINtides inhibit kinase activity with high affinity by binding across the entire substrate binding site and therefore also block GluN2B binding.
“They inhibit kinase activity with high affinity by binding across the entire substrate binding site (FIGURE 2B7) (61, 147, 153), and therefore also block GluN2B binding (152, 154).”
From Synaptic memory and CaMKII (2023) · cites this paper as [153]
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Self-citationStructure–function of the multifunctional Ca2+/calmodulin-dependent protein kinase II
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“They inhibit kinase activity with high af fi nity by binding across the entire substrate binding site ( FIGURE 2 B7 ) (61, 147, 153), and therefore also block GluN2B binding (152, 154).”
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- Authors
- Chang, B. H., Mukherji, S., & Soderling, T. R.
- Affiliations
- Oregon Health & Science University (US)
- Corresponding author
- Soderling, T.R.
- ORCID
- Chang, B.H.
- Venue
- Neuroscience
- Publisher
- Elsevier BV
- Published
- 2001-02
- Volume
- 102
- Issue
- 4
- Pages
- 767-777
- ISSN
- 0306-4522 (ISSN-L)
- OpenAlex
- W1996351506
- Cited by
- 95
- References
- 0
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 4 · 2021: 1 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 9 · 2015: 3 · 2014: 3 · 2013: 4 · 2012: 6
- FWCI
- 1.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- protein isoforms, calcium/calmodulin-dependent protein kinase II, peptide inhibitors, brain localization, hippocampus, cerebellum, inferior colliculus, hippocampal neurons, synapse localization, testis expression, rat brain
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Brain Chemistry, Carrier Proteins, Cells, Cultured, Cloning, Molecular, Hippocampus, Immunohistochemistry, Isomerism, Molecular Sequence Data, Phosphorylation, RNA, Messenger, Gene Expression, In Situ Hybridization, Protein Structure, Tertiary, Calcium-Calmodulin-Dependent Protein Kinases, Intracellular Signaling Peptides and Proteins, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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