Cited by 19Neuroscience and Neuropharmacology ResearchProtein Kinase Regulation and GTPase SignalingGenetics and Neurodevelopmental Disorders

Activity-Dependent Modulation of the Interaction between CaMKIIα and Abi1 and Its Involvement in Spine Maturation

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Park, Esther, Chi, Susan, Park, Dongeun·2012·The Journal of Neuroscience

Abstract

Remodeling of dendritic spines through regulation of actin dynamics is a key event in activity-dependent structural plasticity. However, the molecular mechanism underlying this process is poorly understood. Here, we show that activity-dependent modulation of Abl interactor 1–Ca 2+/calmodulin-dependent kinase IIα (Abi1–CaMKIIα) interaction, and thereby their activity, is important for regulation of spine morphology in cultured rat hippocampal neurons. Abi1 interacts with CaMKIIα at resting conditions through Abi1's tSNARE (target membrane-associated SNARE), which harbors striking homology with CaMKIIα regulatory domain. The interaction of the two proteins, Abi1 and CaMKIIα, results in their simultaneous inhibition, inhibition of CaMKIIα activity, and also inhibition of Abi1-dependent Rac activation. Their functional impediment is released when they dissociate from each other by calmodulin binding through glutamate receptor activation. Before dissociation, Abi1 is phosphorylated by CaMKIIα at serine 88, which may involve in regulation of Rac activation and spine maturation. Our results suggest that modulation of the interaction between Abi1 and CaMKIIα, through the glutamate receptor pathway, may be a molecular mechanism underlying activity-regulated structural plasticity in rat hippocamapal neurons.

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Crossref · 10.1523/jneurosci.2257-12.2012

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  • Ca2+/calmodulin-dependent kinase IIα interacts with ABI1 and phosphorylates Ser88, which may be required for ABI-mediated dendritic spine maturation.

    “Ca2+/calmodulin-dependent kinase IIα (CAMKIIα) interacts with ABI1 and phosphorylates Ser88, which may be required for ABI-mediated dendritic spine maturation51 (Fig. 3d).”

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Authors
Park, E., Chi, S., & Park, D.
Affiliations
  • Seoul National University (KR)
  • Mayo Clinic (US)
Venue
The Journal of Neuroscience
Published
2012-09-19
Volume
32
Issue
38
Pages
13177-13188
ISSN
  • 0270-6474 (ISSN-L)
  • 1529-2401
OpenAlex
W2015119761
Cited by
19
References
3
Citations by year
2025: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 2 · 2014: 5 · 2013: 1
FWCI
1.05
Type
journal article
Language
en
Open access
Locations
  • Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Keywords
ABI1, CaMKIIα, dendritic spine maturation, protein-protein interaction, calmodulin binding, glutamate receptor activation, Rac activation, actin dynamics, hippocampal neurons, synaptic plasticity
MeSH terms
Adenosine Triphosphate, Animals, Calcium, Calcium Chloride, Cells, Cultured, Cerebral Cortex, Embryo, Mammalian, Hippocampus, Humans, Iodine Isotopes, Neurons, Phosphorylation, Protein Binding, Serine, Synapses, Transfection, Ionomycin, N-Methylaspartate, Rats, Sprague-Dawley, Excitatory Amino Acid Agents, Glutamic Acid, Catalytic Domain, RNA, Small Interfering, Immunoprecipitation, Adaptor Proteins, Signal Transducing, Dendritic Spines, Green Fluorescent Proteins, Vesicular Glutamate Transport Protein 1, SNARE Proteins, Qa-SNARE Proteins, Glucose Transporter Type 1, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Calcium Ionophores

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