Protein phosphatase 1 is involved in the dissociation of Ca2+/calmodulin‐dependent protein kinase II from postsynaptic densities
Abstract
Autophosphorylation-dependent translocation of Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) to postsynaptic densities (PSDs) from cytosol may be a physiologically important process during synaptic activation. We investigated a protein phosphatase responsible for dephosphorylation of the kinase. CaM kinase II was shown to be targeted to two sites using the gel overlay method in two-dimensional gel electrophoresis. Protein phosphatase 1 (PP1) was identified to dephosphorylate CaM kinase II from its complex with PSDs using phosphatase inhibitors and activators, and purified phosphatases. The kinase was released from PSDs after its dephosphorylation by PP1.
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PP1 enhances dissociation of autophosphorylated CaMKII from the PSD.
“In addition, PP1 has been shown to enhance dissociation of autophosphorylated CaMKII from the PSD (386).”
From Synaptic memory and CaMKII (2023) · cites this paper as [386]
PP1 is the likely phosphatase for preventing spread of CaMKII active state, as it is concentrated in the PSD, whereas PP2A is abundant in cytoplasm, and CaMKII in PSD is preferentially dephosphorylated by PP1.
“PP1 is the likely phosphatase for such a role, as it is concentrated in the PSD, whereas PP2A is abundant in the cytoplasm (64, 385, 386) and CaMKII in the PSD is preferentially dephosphorylated by PP1 (385).”
From Synaptic memory and CaMKII (2023) · cites this paper as [386]
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“In addition, PP1 has been shown to enhance dissociation of autophosphorylated CaMKII from the PSD (386).”
BackgroundYoshimura, 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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- Authors
- Yoshimura, Y., Sogawa, Y., & Yamauchi, T.
- Affiliations
- Tokushima University (JP)
- Corresponding author
- Yamauchi, Takashi
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-03-12
- Volume
- 446
- Issue
- 2-3
- Pages
- 239-242
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2027177990
- Cited by
- 48
- References
- 0
- Citations by year
- 2023: 1 · 2021: 2 · 2017: 3 · 2015: 3 · 2014: 2 · 2013: 1 · 2012: 1
- FWCI
- 1.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (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 › Protein Tyrosine Phosphatases
- Keywords
- protein phosphatase 1, calcium/calmodulin-dependent protein kinase II, postsynaptic density, dephosphorylation, autophosphorylation, kinase translocation, synaptic plasticity, phosphatase inhibitors
- MeSH terms
- Animals, Calcium, Humans, Phosphoprotein Phosphatases, Recombinant Proteins, Synapses, Calcium-Calmodulin-Dependent Protein Kinases, Rats, Protein Phosphatase 1, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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