ArticleThe Journal of biological chemistry2012
Calcyon forms a novel ternary complex with dopamine D1 receptor through PSD-95 protein and plays a role in dopamine receptor internalization.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
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- Role of Glutamate Receptor-related Biomarkers in the Etiopathogenesis of ADHD.Clinical psychopharmacology and neuroscience : the official scientific journal of the Korean College of Neuropsychopharmacology · 2024Article
- ΔInternational journal of molecular sciences · 2023Article
- Transcriptome Profiling of the Dorsomedial Prefrontal Cortex in Suicide Victims.International journal of molecular sciences · 2022Article
- Article
- Physiological and Functional Basis of Dopamine Receptors and Their Role in Neurogenesis: Possible Implication for Parkinson's disease.Journal of experimental neuroscience · 2018Article
- Dynein binds and stimulates axonal motility of the endosome adaptor and NEEP21 family member, calcyon.The international journal of biochemistry & cell biology · 2017Article
- Stress and corticosterone alter synaptic plasticity in a rat model of Parkinson's disease.Neuroscience letters · 2017Article
- Posttranslational Modifications Regulate the Postsynaptic Localization of PSD-95.Molecular neurobiology · 2017Review
- MicroRNAs in Schizophrenia: Implications for Synaptic Plasticity and Dopamine-Glutamate Interaction at the Postsynaptic Density. New Avenues for Antipsychotic Treatment Under a Theranostic Perspective.Molecular neurobiology · 2015Review
- In adult female hamsters hypothyroidism stimulates D1 receptor-mediated breathing without altering D1 receptor expression.Respiratory physiology & neurobiology · 2015Article
- Dopamine Receptors and Neurodegeneration.Aging and disease · 2015Review
- New therapeutic strategies targeting D1-type dopamine receptors for neuropsychiatric disease.Frontiers in biology · 2015Article
- Postsynaptic Density Protein 95 in the Striosome and Matrix Compartments of the Human Neostriatum.Frontiers in neuroanatomy · 2015Article
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Authors and funding
8 authors at 7 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calcyon, once known for interacting directly with the dopamine D(1) receptor (D(1)DR), is implicated in various neuropsychiatric disorders including schizophrenia, bipolar disorder, and attention deficit hyperactivity disorder. Although its direct interaction with D(1)DR has been shown to be misinterpreted, it still plays important roles in D(1)DR signaling. Here, we found that calcyon interacts with the PSD-95 and subsequently forms a ternary complex with D(1)DR through PSD-95. Calcyon is phosphorylated on Ser-169 by the PKC activator phorbol 12-myristate 13-acetate or by the D(1)DR agonist SKF-81297, and its phosphorylation increases its association with PSD-95 and recruitment to the cell surface. Interestingly, the internalization of D(1)DR at the cell surface was enhanced by phorbol 12-myristate 13-acetate and SKF-81297 in the presence of calcyon, but not in the presence of its S169A phospho-deficient mutant, suggesting that the phosphorylation of calcyon and the internalization of the surface D(1)DR are tightly correlated. Our results suggest that calcyon regulates D(1)DR trafficking by forming a ternary complex with D(1)DR through PSD-95 and thus possibly linking glutamatergic and dopamine receptor signalings. This also raises the possibility that a novel ternary complex could represent a potential therapeutic target for the modulation of related neuropsychiatric disorders.
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