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Cited by 72Neuroscience and Neuropharmacology ResearchProtein Kinase Regulation and GTPase SignalingSignaling Pathways in Disease

Investigation of protein substrates of Ca2+/calmodulin-dependent protein kinase II translocated to the postsynaptic density

Yoshimura, Yoshiyuki, Aoi, Chiaki, Yamauchi, Takashi·2000·Molecular Brain Research
DOI 10.1016/s0169-328x(00)00170-4
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Abstract

To elucidate the physiological significance of the translocation of Ca(2+)/calmodulin-dependent protein kinase II (CaM kinase II), we investigated substrates of CaM kinase II in the postsynaptic density (PSD). PSD proteins were phosphorylated by CaM kinase II of its PSD complex, and separated by two-dimensional gel electrophoresis. More than 28 proteins were phosphorylated under experimental conditions. Proteins corresponding to CaM kinase II substrates were excised from the gels, eluted electrophoretically, and then sequenced. Several substrates were identified, including PSD95, SAP90, alpha-internexin, neurofilament L chain, cAMP phosphodiesterase, and alpha- and beta-tubulin. Some substrates were also identified by immunoblotting, including N-methyl-D-aspartic acid (NMDA) receptor 2B subunit, 1-alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor 1 (GluR1), neurofilament H chain and dynamin. PSD95, SAP90, dynamin, and alpha-internexin were demonstrated for the first time to be substrates of CaM kinase II. NMDA receptor 2B subunit and GluR1 existed as major substrates in the PSD. Moreover, translocation of CaM kinase II was inhibited by phosphorylation of PSD proteins. These results suggest that CaM kinase II plays important roles in the regulation of synaptic functions through phosphorylation of PSD proteins.

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  • Although it is well established that CaMKII phosphorylates numerous synaptic proteins, an essential role for CaMKII phosphorylation of many of these targets largely remains elusive.

    “It should be pointed out that, although it is well established that CaMKII phosphorylates numerous synaptic proteins (66, 434–437), as reviewed here, despite intensive research an essential role for CaMKII phosphorylation of many of these targets largely remains elusive.”

    From Synaptic memory and CaMKII (2023) · cites this paper as [434]

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Authors
Yoshimura, Y., Aoi, C., & Yamauchi, T.
Affiliations
Tokushima University (JP)
Corresponding author
Yamauchi, Takashi
Venue
Molecular Brain Research
Publisher
Elsevier BV
Published
2000-09
Volume
81
Issue
1-2
Pages
118-128
ISSN
0169-328X (ISSN-L)
DOI
10.1016/s0169-328x(00)00170-4
OpenAlex
W2007309241
Cited by
72
References
45
Citations by year
2023: 1 · 2017: 1 · 2015: 3 · 2014: 1 · 2013: 3 · 2012: 6
FWCI
2.19
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Molecular Brain Research (publishedVersion)
  • PubMed (publishedVersion)
Funders
Ministry of Education, Culture, Sports, Science and Technology
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, protein phosphorylation, kinase substrates, PSD-95, alpha-internexin, dynamin, NMDA receptor NR2B, GluR1, AMPA receptors, neurofilaments, cAMP phosphodiesterase, tubulin
MeSH terms
Disks Large Homolog 4 Protein, Amino Acid Sequence, Animals, Kinetics, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Peptide Fragments, Phosphorylation, Substrate Specificity, Synapses, Electrophoresis, Gel, Two-Dimensional, Prosencephalon, Calcium-Calmodulin-Dependent Protein Kinases, Receptors, AMPA, Intracellular Signaling Peptides and Proteins, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2

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