ArticleThe Journal of biological chemistry2015
Glycogen Synthase Kinase 3β-mediated Phosphorylation in the Most C-terminal Region of Protein Interacting with C Kinase 1 (PICK1) Regulates the Binding of PICK1 to Glutamate Receptor Subunit GluA2.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- The medial septum-hippocampus-lateral septum circuitry in spatial memory: linking healthy function to early Alzheimer's disease and translational opportunities.Translational neurodegeneration · 2025Review
- AMPA Receptors in Synaptic Plasticity, Memory Function, and Brain Diseases.Cellular and molecular neurobiology · 2025Review
- Alzheimer's disease as a synaptopathy: Evidence for dysfunction of synapses during disease progression.Frontiers in synaptic neuroscience · 2023Review
- GSK-3β Disrupts Neuronal Oscillatory Function to Inhibit Learning and Memory in Male Rats.Cellular and molecular neurobiology · 2022Article
- NMDA and AMPA Receptors at Synapses: Novel Targets for Tau and α-Synuclein Proteinopathies.Biomedicines · 2022Review
- The role of pathological tau in synaptic dysfunction in Alzheimer's diseases.Translational neurodegeneration · 2021Review
- FSC231 alleviates paclitaxel-induced neuralgia by inhibiting the interactions between PICK1 and GluA2 and activates GSK-3β and ERK1/2.Brain and behavior · 2021Article
- Long-term depression-related tau phosphorylation is enhanced by methylene blue in healthy rat hippocampus.Pharmacological reports : PR · 2021Article
- Inhibition of AKT/GSK3β/CREB Pathway Improves the Responsiveness to AMPA Receptor Antagonists by Regulating GRIA1 Surface Expression in Chronic Epilepsy Rats.Biomedicines · 2021Article
- Review
- GSK3α, not GSK3β, drives hippocampal NMDAR-dependent LTD via tau-mediated spine anchoring.The EMBO journal · 2021Article
- Pharmacological inhibition of glycogen synthase kinase 3 increases operant alcohol self-administration in a manner associated with altered pGSK-3β, protein interacting with C kinase and GluA2 protein expression in the reward pathway of male C57BL/6J mice.Behavioural pharmacology · 2020Article
- Coordination of AMPA receptor trafficking by Rab GTPases.Small GTPases · 2019Review
- PDZ Domains as Drug Targets.Advanced therapeutics · 2019Review
- AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking.Cellular and molecular life sciences : CMLS · 2019Review
- Genetic Analysis ofFrontiers in neurology · 2018Article
- Intermittent hypoxia produces Alzheimer disease?Oncotarget · 2017Article
- PICK1 Genetic Variation and Cognitive Function in Patients with Schizophrenia.Scientific reports · 2017Article
- Treatment of intermittent hypoxia increases phosphorylated tau in the hippocampus via biological processes common to aging.Molecular brain · 2017Article
- Amyloid-β-Induced Dysregulation of AMPA Receptor Trafficking.Neural plasticity · 2016Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein interacting with C kinase 1 (PICK1) is a synaptic protein interacting with the AMPA receptor subunits GluA2/3. The interaction between GluA2 and PICK1 is required for the removal of GluA2 from the synaptic plasma membrane during long-term depression (LTD). It has been suggested that glycogen synthase kinase 3β (GSK-3β) is activated during LTD, but the relationships between GluA2, PICK1, and GSK-3β are not well understood. In particular, the substrate(s) of GSK-3β have not yet been determined. Here we showed that PICK1 is a substrate of GSK-3β. We found that Ser(339), Ser(342), Ser(412), and Ser(416) of PICK1 were putative GSK-3β-mediated phosphorylation sites. Among these sites, Ser(416) played a crucial role in regulating the interaction between GluA2 and PICK1. We showed that replacing Ser(416) with Ala disrupted the GluA2-PICK1 interaction, whereas substituting Ser(416) with Glu or Asp retained this interaction. However, deletion of Ser(416) did not affect the GluA2-PICK1 interaction, and substitution of Ser(416) with Ala did not alter the PICK1-PICK1 interaction. Using image analysis in COS-7 cells with AcGFP1-fused PICK1, we showed that substitution of Ser(416) with Ala increased the formation of AcGFP1-positive clusters, suggesting an increase in the association of PICK1 with the membrane. This may have resulted in the dissociation of the GluA2-PICK1 complexes. Our results indicated that GSK-3β-mediated phosphorylation of PICK1 at Ser(416) was required for its association with the AMPA receptor subunit. Therefore, the GSK-3β-mediated phosphorylation of PICK1 may be a regulating factor during LTD induction.
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