ArticleThe Journal of biological chemistry2013
Casein kinase 2 phosphorylation of protein kinase C and casein kinase 2 substrate in neurons (PACSIN) 1 protein regulates neuronal spine formation.
Article in The Journal of biological chemistry, 2013. 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, 29 citations in OpenAlex.
- Male caregiving experience alters hippocampal neuroplasticity and transcription independent of reproduction in a biparental species.Communications biology · 2025Article
- Article
- Function of SYDE C2-RhoGAP family as signaling hubs for neuronal development deduced by computational analysis.Scientific reports · 2022Article
- PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022Review
- Regulation of Synapse Weakening through Interactions of the Microtubule Associated Protein Tau with PACSIN1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Synaptic AP2 CCV life cycle regulation by the Eps15, ITSN1, Sgip1/AP2, synaptojanin1 interactome.Scientific reports · 2021Article
- Small molecule induces mitochondrial fusion for neuroprotection via targeting CK2 without affecting its conventional kinase activity.Signal transduction and targeted therapy · 2021Article
- Phosphorylation of unique C-terminal sites of the mu-opioid receptor variants 1B2 and 1C1 influences their Gs association following chronic morphine.Journal of neurochemistry · 2020Article
- Gene domain-specific DNA methylation episignatures highlight distinct molecular entities of ADNP syndrome.Clinical epigenetics · 2019Article
- Reciprocal Regulation of KCC2 Trafficking and Synaptic Activity.Frontiers in cellular neuroscience · 2019Review
- DNA methylation and substance-use risk: a prospective, genome-wide study spanning gestation to adolescence.Translational psychiatry · 2016Article
- Bromodomain and extra-terminal (BET) family proteins: New therapeutic targets in major diseases.Journal of biosciences · 2016Review
- Neuroproteomics and Systems Biology Approach to Identify Temporal Biomarker Changes Post Experimental Traumatic Brain Injury in Rats.Frontiers in neurology · 2016Article
- BET protein Brd4 activates transcription in neurons and BET inhibitor Jq1 blocks memory in mice.Nature neuroscience · 2015Article
- Regulating Rac in the nervous system: molecular function and disease implication of Rac GEFs and GAPs.BioMed research international · 2015Review
- ProSAP1 and membrane nanodomain-associated syndapin I promote postsynapse formation and function.The Journal of cell biology · 2014Article
- Lipidomic mass spectrometry and its application in neuroscience.World journal of biological chemistry · 2013Review
- Polyglutamine domain flexibility mediates the proximity between flanking sequences in huntingtin.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- PICK1 interacts with PACSIN to regulate AMPA receptor internalization and cerebellar long-term depression.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- GluN3A: an NMDA receptor subunit with exquisite properties and functions.Neural plasticity · 2013Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The PACSIN (protein kinase C and casein kinase 2 substrate in neurons) adapter proteins couple components of the clathrin-mediated endocytosis machinery with regulators of actin polymerization and thereby regulate the surface expression of specific receptors. The brain-specific PACSIN 1 is enriched at synapses and has been proposed to affect neuromorphogenesis and the formation and maturation of dendritic spines. In studies of how phosphorylation of PACSIN 1 contributes to neuronal function, we identified serine 358 as a specific site used by casein kinase 2 (CK2) in vitro and in vivo. Phosphorylated PACSIN 1 was found in neuronal cytosol and membrane fractions. This localization could be modulated by trophic factors such as brain-derived neurotrophic factor (BDNF). We further show that expression of a phospho-negative PACSIN 1 mutant, S358A, or inhibition of CK2 drastically reduces spine formation in neurons. We identified a novel protein complex containing the spine regulator Rac1, its GTPase-activating protein neuron-associated developmentally regulated protein (NADRIN), and PACSIN 1. CK2 phosphorylation of PACSIN 1 leads to a dissociation of the complex upon BDNF treatment and induces Rac1-dependent spine formation in dendrites of hippocampal neurons. These findings suggest that upon BDNF signaling PACSIN 1 is phosphorylated by CK2 which is essential for spine formation.
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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 OpenQuestion graph.