Ca2+-PP2B-PSD-95 axis: A novel regulatory mechanism of the phosphorylation state of Serine 295 of PSD-95.

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In one paragraph

Article in PloS one, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Takahiko ChimuraDepartment of Basic Medical Sciences, Institute of Medical Science, Division of Neuronal Network, University of Tokyo, Tokyo, Japan.ORCID 0009-0006-5776-816X

Toshiya ManabeDepartment of Basic Medical Sciences, Institute of Medical Science, Division of Neuronal Network, University of Tokyo, Tokyo, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The phosphorylation state of PSD-95 at Serine 295 (Ser295) is important for the regulation of synaptic plasticity. Although the activation of NMDA receptors (NMDARs), which initiates an intracellular calcium signaling cascade, decreases phosphorylated Ser295 (pS295) of PSD-95, the molecular mechanisms are not fully understood. We found that the calcium-activated protein phosphatase PP2B dephosphorylated pS295 not only in basal conditions but also in NMDAR-activated conditions in cultured neurons. The biochemical assay also revealed the dephosphorylation of pS295 by PP2B, consistently supporting the results obtained using neurons. The newly identified calcium signaling cascade "Ca2+-PP2B-PSD-95 axis" would play an important role in the molecular mechanism for NMDA receptor-dependent plasticity.

Indexed as

CalciumDisks Large Homolog 4 ProteinNeuronsReceptors, N-Methyl-D-AspartateSerineAnimalsCalcium SignalingCells, CulturedHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsPhosphoprotein PhosphatasesPhosphorylationRatsCalciumDisks Large Homolog 4 ProteinDlg4 protein, ratIntracellular Signaling Peptides and ProteinsMembrane ProteinsPhosphoprotein PhosphatasesReceptors, N-Methyl-D-AspartateSerine

Identifiers

PMID39509447

DOI10.1371/journal.pone.0313441

PMCPMC11542788

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.