Reciprocal Activation within a Kinase-Effector Complex Underlying Persistence of Structural LTP
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Long-term synaptic plasticity requires a mechanism that converts short Ca 2+ pulses into persistent biochemical signaling to maintain changes in the synaptic structure and function. Here, we present a novel mechanism of a positive feedback loop, formed by a reciprocally activating kinase-effector complex (RAKEC) in dendritic spines, enabling the persistence and confinement of a molecular memory. We found that stimulation of a single spine causes the rapid formation of a RAKEC consisting of CaMKII and Tiam1, a Rac-GEF. This interaction is mediated by a pseudo-autoinhibitory domain on Tiam1, which is homologous to the CaMKII autoinhibitory domain itself. Therefore, Tiam1 binding results in constitutive CaMKII activation, which in turn persistently phosphorylates Tiam1. Phosphorylated Tiam1 promotes stable actin-polymerization through Rac1, thereby maintaining the structure of the spine during LTP. The RAKEC can store biochemical information in small subcellular compartments, thus potentially serving as a general mechanism for prolonged and compartmentalized signaling.
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Tiam1 has a CaMKII binding domain homologous to the GluN2B CTD, and Tiam1-CaMKII complex formation results in constitutive CaMKII activity.
“The authors find that Tiam1 has a CaMKII binding domain. This domain is homologous to the GluN2B CTD, and thus the Tiam1-CaMKII complex formation results in constitutive CaMKII activity.”
From Synaptic memory and CaMKII (2023) · cites this paper as [314]
The Results sections on Tiam1 binding and reciprocal activation (page unavailable) identify a CaMKII-binding region in Tiam1 and report that the formed complex maintains CaMKII activity without Ca2+/calmodulin. They describe that region as homologous to CaMKII’s autoinhibitory domain, not to the GluN2B C-terminal domain. The claimed GluN2B homology is therefore unsupported by our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredRhoGEFs kalirin-7, Trio, and Tiam are expressed in spines and phosphorylated by CaMKII.
“The RhoGEFs that have received the most attention are kalirin-7, Trio, and Tiam, which are all expressed in spines and phosphorylated by CaMKII (314–317).”
From Synaptic memory and CaMKII (2023) · cites this paper as [314]
The Introduction describes Tiam1 and Kalirin-7/Trio as CaMKII substrates involved in spine formation and development. The Results place Tiam1 in a stimulated spine, but the cited passages do not establish that all three are expressed in spines; the paper also does not say they have received the most attention. (LLM, conf=0.78)
Experimental — accuracy not yet measuredCaMKII phosphorylates Tiam1.
“CaMKII, in turn, phosphorylates Tiam1.”
From Synaptic memory and CaMKII (2023) · cites this paper as [314]
There is compelling evidence that CaMKII, via phosphorylation, initiates a series of actin-based cytoskeletal rearrangements in the spine.
“Indeed, there is compelling evidence that CaMKII, via phosphorylation, initiates a series of actin-based cytoskeletal rearrangements in the spine (32, 312–314).”
From Synaptic memory and CaMKII (2023) · cites this paper as [314]
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The role of CaMKII autophosphorylation for NMDA receptor-dependent synaptic potentiation
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Mechanical regulation of synapse formation and plasticity
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Rac1 is a downstream effector of PKCα in structural synaptic plasticity
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Tiam1 is Critical for Glutamatergic Synapse Structure and Function in the Hippocampus
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Imaging dendritic spines: molecular organization and signaling for plasticity
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Endophilin A1 drives acute structural plasticity of dendritic spines in response to Ca2+/calmodulin
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The role of molecular diffusion within dendritic spines in synaptic function
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Single Synapse LTP: A Matter of Context?
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Self-citationEngineering memory with an extrinsically disordered kinase
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Roles of Rac1-Dependent Intrinsic Forgetting in Memory-Related Brain Disorders: Demon or Angel
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A Lipid-Raft Theory of Alzheimer's Disease
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Multiphasic protein condensation governed by shape and valency
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Self-citationPalmitoylated Proteins in Dendritic Spine Remodeling
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Self-citationAlteration of synaptic protein composition during developmental synapse maturation
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Self-citationLoss of the polarity protein Par3 promotes dendritic spine neoteny and enhances learning and memory
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MARCKS and PI(4,5)P2 reciprocally regulate actin-based dendritic spine morphology
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Activity-Dependent Stabilization of Nascent Dendritic Spines Requires Nonenzymatic CaMKIIα Function
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Regulation of Presynaptic Release Machinery by Cell Adhesion Molecules
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The Janus face of CaMKII: from memory consolidation to neurotoxic switch in Alzheimer’s disease
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Synaptic Plasticity in the Hippocampus
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Presynaptic Rac1 in the hippocampus selectively regulates working memory
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Molecular Underpinnings of Memory Persistence and Forgetting
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Synaptic Tagging and Capture: Functional Implications and Molecular Mechanisms
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LOV2-based photoactivatable CaMKII and its application to single synapses: Local Optogenetics
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Activity-dependent regulation of Cdc42 by Ephexin5 drives synapse growth and stabilization
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A lipid-raft theory of Alzheimer's disease
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Ras-related C3 botulinum toxin substrate 1 role in pathophysiology of neurological diseases
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Self-citationMolecular Mechanisms Underlying Synaptic Tagging and Consolidation
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NMDAR Phosphoproteome Controls Synaptic Growth and LearningPreprint
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Presynaptic Rac1 in the hippocampus selectively regulates working memoryPreprint
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Presynaptic Rac1 in the hippocampus selectively regulates working memoryPreprint
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CaMKII activation triggers persistent formation and segregation of postsynaptic liquid phase
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Calcium | Calcium/Calmodulin-Dependent Protein Kinase II
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- Authors
- Saneyoshi, T., Matsuno, H., Suzuki, A., Murakoshi, H., Hedrick, N. G., Agnello, E., O’Connell, R., Stratton, M. M., Yasuda, R., & Hayashi, Y.
- Affiliations
- Kyoto University (JP)
- RIKEN Center for Brain Science (JP)
- Max Planck Florida Institute for Neuroscience (US)
- Duke University (US)
- University of Massachusetts Amherst (US)
- South China Normal University (CN)
- Corresponding author
- Saneyoshi, Takeo
- Hayashi, Yasunori
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2019-06
- Volume
- 102
- Issue
- 6
- Pages
- 1199-1210.e6
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC6669903
- OpenAlex
- W2944452573
- Cited by
- 119
- References
- 67
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 26 · 2023: 19 · 2022: 14 · 2021: 21 · 2020: 14 · 2019: 5 · 2014: 1
- FWCI
- 6.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
- Funders
- Kyoto University Education and Research Foundation
- Human Frontier Science Program
- NOVARTIS Foundation (Japan) for the Promotion of Science
- Ministry of Education, Culture, Sports, Science and Technology (374539, 18H04733, 22110006, 817144, 20240032, 1031691, 854508, 16H02455, 18H05434)
- Takeda Science Foundation
- RIKEN
- Takeda Pharmaceutical Company
- Japan Foundation for Applied Enzymology
- Naito Foundation
- Brain Science Foundation
- Research Foundation for Opto-Science and Technology
- National Institutes of Health (R01DA17310, DP1-NS096787, R01-MH080047)
- Uehara Memorial Foundation
- Fujitsu
- 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 › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Keywords
- long-term potentiation, dendritic spines, CaMKII, Tiam1, positive feedback loop, actin polymerization, Rac1, synaptic plasticity, molecular memory, compartmentalized signaling
- MeSH terms
- T-Lymphoma Invasion and Metastasis-inducing Protein 1, Actins, Animals, Hippocampus, Neurons, Phosphorylation, Pyrones, Quinolines, Long-Term Potentiation, Microscopy, Confocal, Guanine Nucleotide Exchange Factors, rac1 GTP-Binding Protein, Feedback, Physiological, Dendritic Spines, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Polymerization
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