Identification of Protein Substrates of Ca2+/Calmodulin-Dependent Protein Kinase II in the Postsynaptic Density by Protein Sequencing and Mass Spectrometry
Abstract
Previously we detected more than 28 PSD proteins to be phosphorylated by CaM kinase II, and identified 14 protein substrates (Yoshimura, Y., Aoi, T., Yamauchi, T., Mol. Brain Res. 81, 118-128, 2000). In the present study, the remaining substrates were analyzed by protein sequencing and mass spectrometry. We found 6 proteins not previously known to be substrates of CaM kinase II, namely PSD95-associated protein, SAP97, TOAD-64, TNF receptor-associated protein, insulin-receptor tyrosine kinase 58/53 kDa substrate, and homer 1b.
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CaMKII is a calcium-activated kinase involved in structural plasticity by remodeling of the postsynaptic density, rearrangement of the actin cytoskeleton and maintenance of spine enlargement.
“CaMKII is a calcium-activated kinase involved in structural plasticity by remodeling of the postsynaptic density (Yoshimura et al., 2002), rearrangement of the actin cytoskeleton (Okamoto et al., 2007) and maintenance of spine enlargement (Matsuzaki et al., 2004; Lee et al., 2009).”
From Barriers in the brain: resolving dendritic spine morphology and compartmentalization (2014) · cites this paper as Yoshimura et al., 2002
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Tu, J. C., Xiao, B., Yuan, J. P., Lanahan, A. A., Leoffert, K., Li, M., Linden, D. J., & Worley, P. F. (1998) · Neuron · doi:10.1016/s0896-6273(00)80589-9 · Cited by 862 · see citing works
Yoshimura, Y., Aoi, C., & Yamauchi, T. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00170-4 · Cited by 72 · see citing works
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“CaMKII is a calcium-activated kinase involved in structural plasticity by remodeling of the postsynaptic density (Yoshimura et al., 2002), rearrangement of the actin cytoskeleton (Okamoto et al., 2007) and maintenance of spine enlargement (Matsuzaki et al., 2004; Lee et al., 2009).”
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Iasevoli, F., Polese, D., Ambesi-Impiombato, A., Muscettola, G., & de Bartolomeis, A. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.01.041 · Cited by 40 · see citing works
- Authors
- Yoshimura, Y., Shinkawa, T., Taoka, M., Kobayashi, K., Isobe, T., & Yamauchi, T.
- Affiliations
- Tokushima University (JP)
- Ministry of Education, Culture, Sports, Science and Technology (JP)
- Tokyo Metropolitan University (JP)
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2002-01
- Volume
- 290
- Issue
- 3
- Pages
- 948-954
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2058569653
- Cited by
- 94
- References
- 2
- Citations by year
- 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2019: 1 · 2017: 2 · 2015: 2 · 2014: 3 · 2013: 5 · 2012: 5
- FWCI
- 2.79
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- 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
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- calcium/calmodulin-dependent protein kinase II, protein substrates, postsynaptic density, protein phosphorylation, SAP97, insulin receptor substrate, synaptic proteins
- MeSH terms
- Amino Acid Sequence, Animals, Models, Neurological, Molecular Sequence Data, Nerve Tissue Proteins, Phosphorylation, Mass Spectrometry, Synapses, Electrophoresis, Gel, Two-Dimensional, Calcium-Calmodulin-Dependent Protein Kinases, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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