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Reciprocal Activation within a Kinase-Effector Complex Underlying Persistence of Structural LTP
Open accessAbstract
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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“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]
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“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]
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“CaMKII, in turn, phosphorylates Tiam1.”
From Synaptic memory and CaMKII (2023) · cites this paper as [314]
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“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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Cites
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
Germline Transmission and Tissue-Specific Expression of Transgenes Delivered by Lentiviral Vectors
Lois, C., Hong, E. J., Pease, S., Brown, E. J., & Baltimore, D. (2002) · Science · doi:10.1126/science.1067081 · Cited by 1,992
The molecular basis of CaMKII function in synaptic and behavioural memory
Lisman, J., Schulman, H., & Cline, H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn753 · Cited by 1,860
The Conformational Plasticity of Protein Kinases
Huse, M., & Kuriyan, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00741-9 · Cited by 1,760
Emergent Properties of Networks of Biological Signaling Pathways
Bhalla, U. S., & Iyengar, R. (1999) · Science · doi:10.1126/science.283.5400.381 · Cited by 1,686
Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
Barria, A., Muller, D., Derkach, V., Griffith, L. C., & Soderling, T. R. (1997) · Science · doi:10.1126/science.276.5321.2042 · Cited by 1,049
The Postsynaptic Architecture of Excitatory Synapses: A More Quantitative View
Sheng, M., & Hoogenraad, C. C. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.060805.160029 · Cited by 1,003
Okamoto, K.-I., Nagai, T., Miyawaki, A., & Hayashi, Y. (2004) · Nature Neuroscience · doi:10.1038/nn1311 · Cited by 854
Self-citationA Brief History of Long-Term Potentiation
Nicoll, R. A. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.015 · Cited by 841
Interaction with the NMDA receptor locks CaMKII in an active conformation
Bayer, K.-U., De Koninck, P., Leonard, A. S., Hell, J. W., & Schulman, H. (2001) · Nature · doi:10.1038/35081080 · Cited by 732
NMDA Receptor Subunit Composition Controls Synaptic Plasticity by Regulating Binding to CaMKII
Barria, A., & Malinow, R. (2005) · Neuron · doi:10.1016/j.neuron.2005.08.034 · Cited by 709
Activation of CaMKII in single dendritic spines during long-term potentiation
Lee, S.-J. R., Escobedo-Lozoya, Y., Szatmari, E. M., & Yasuda, R. (2009) · Nature · doi:10.1038/nature07842 · Cited by 685
Self-citationShen, K., & Meyer, T. (1999) · Science · doi:10.1126/science.284.5411.162 · Cited by 673
Structural and Molecular Remodeling of Dendritic Spine Substructures during Long-Term Potentiation
Bosch, M., Castro, J., Saneyoshi, T., Matsuno, H., Sur, M., & Hayashi, Y. (2014) · Neuron · doi:10.1016/j.neuron.2014.03.021 · Cited by 637
Self-citationThe Spread of Ras Activity Triggered by Activation of a Single Dendritic Spine
Harvey, C. D., Yasuda, R., Zhong, H., & Svoboda, K. (2008) · Science · doi:10.1126/science.1159675 · Cited by 434
Self-citationTashiro, A. (2000) · Cerebral Cortex · doi:10.1093/cercor/10.10.927 · Cited by 416
Structural plasticity of dendritic spines
Bosch, M., & Hayashi, Y. (2012) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.09.002 · Cited by 415
Self-citationKalirin-7 Controls Activity-Dependent Structural and Functional Plasticity of Dendritic Spines
Xie, Z., Srivastava, D. P., Photowala, H., Kai, L., Cahill, M. E., Woolfrey, K. M., Shum, C. Y., Surmeier, D. J., & Penzes, P. (2007) · Neuron · doi:10.1016/j.neuron.2007.10.005 · Cited by 373
Tolias, K. F., Bikoff, J. B., Burette, A., Paradis, S., Harrar, D., Tavazoie, S., Weinberg, R. J., & Greenberg, M. E. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.024 · Cited by 365
CaMKII: Claiming Center Stage in Postsynaptic Function and Organization
Hell, J. W. (2014) · Neuron · doi:10.1016/j.neuron.2013.12.024 · Cited by 364
Shutes, A., Onesto, C., Picard, V., Leblond, B., Schweighoffer, F., & Der, C. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703571200 · Cited by 336
Protein kinases. Regulation by autoinhibitory domains.
Soderling, T. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39900-4 · Cited by 313
Shen, L., Liang, F., Walensky, L. D., & Huganir, R. L. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-21-07932.2000 · Cited by 305
Transition from Reversible to Persistent Binding of CaMKII to Postsynaptic Sites and NR2B
Bayer, K. U., LeBel, É., McDonald, G. L., O’Leary, H., Schulman, H., & Koninck, P. D. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3116-05.2006 · Cited by 259
Otmakhov, N., Tao-Cheng, J.-H., Carpenter, S., Asrican, B., Dosemeci, A., Reese, T. S., & Lisman, J. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.2350-04.2004 · Cited by 258
Chao, L. H., Stratton, M. M., Lee, I., Rosenberg, O. S., Levitz, J., Mandell, D. J., Kortemme, T., Groves, J. T., Schulman, H., & Kuriyan, J. (2011) · Cell · doi:10.1016/j.cell.2011.07.038 · Cited by 258
Self-citationRho GTPase complementation underlies BDNF-dependent homo- and heterosynaptic plasticity
Hedrick, N. G., Harward, S. C., Hall, C. E., Murakoshi, H., McNamara, J. O., & Yasuda, R. (2016) · Nature · doi:10.1038/nature19784 · Cited by 244
Self-citationCaMKII binding to GluN2B is critical during memory consolidation
Halt, A. R., Dallapiazza, R. F., Zhou, Y., Stein, I. S., Qian, H., Juntti, S., Wojcik, S., Brose, N., Silva, A. J., & Hell, J. W. (2012) · The EMBO Journal · doi:10.1038/emboj.2011.482 · Cited by 243
Saneyoshi, T., Wayman, G. A., Fortin, D. A., Davare, M. A., Hoshi, N., Nozaki, N., Natsume, T., & Soderling, T. R. (2008) · Neuron · doi:10.1016/j.neuron.2007.11.016 · Cited by 234
Self-citationAutoinhibitory Domains: Modular Effectors of Cellular Regulation
Pufall, M. A., & Graves, B. J. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.031502.133614 · Cited by 232
Characterization of a calmodulin kinase II inhibitor protein in brain
Chang, B. H., Mukherji, S., & Soderling, T. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10890 · Cited by 227
Fortin, D. A., Davare, M. A., Srivastava, T., Brady, J. D., Nygaard, S. C., Derkach, V. A., & Soderling, T. R. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1746-10.2010 · Cited by 200
Miller, P., Zhabotinsky, A. M., Lisman, J. E., & Wang, X.-J. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030107 · Cited by 199
Analysis of Activated GAPs and GEFs in Cell Lysates
García‐Mata, R., Wennerberg, K., Arthur, W. T., Hooten, N. N., Ellerbroek, S. M., & Burridge, K. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)06031-9 · Cited by 191
Dual Mechanism of a Natural CaMKII Inhibitor
Vest, R. S., Davies, K. D., O’Leary, H., Port, J. D., & Bayer, K. U. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-02-0185 · Cited by 188
Walikonis, R. S., Oguni, A., Khorosheva, E. M., Jeng, C.-J., Asuncion, F. J., & Kennedy, M. B. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00423.2001 · Cited by 181
Incontro, S., Díaz-Alonso, J., Iafrati, J., Vieira, M., Asensio, C. S., Sohal, V. S., Roche, K. W., Bender, K. J., & Nicoll, R. A. (2018) · Nature Communications · doi:10.1038/s41467-018-04439-7 · Cited by 171
Ca2+/Calmodulin-dependent Protein Kinase II Regulates Tiam1 by Reversible Protein Phosphorylation
Fleming, I. N., Elliott, C. M., Buchanan, F. G., Downes, C. P., & Exton, J. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12753 · Cited by 169
Bistability in the Ca2+/Calmodulin-Dependent Protein Kinase-Phosphatase System
Zhabotinsky, A. M. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76469-1 · Cited by 161
Chang, J.-Y., Parra-Bueno, P., Laviv, T., Szatmari, E. M., Lee, S.-J. R., & Yasuda, R. (2017) · Neuron · doi:10.1016/j.neuron.2017.04.041 · Cited by 161
Self-citationVisualization of Synaptic Ca2+/Calmodulin-Dependent Protein Kinase II Activity in Living Neurons
Takao, K., Okamoto, K., Nakagawa, T., Neve, R. L., Nagai, T., Miyawaki, A., Hashikawa, T., Kobayashi, S., & Hayashi, Y. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0085-05.2005 · Cited by 146
Self-citationYamagata, Y., Kobayashi, S., Umeda, T., Inoue, A., Sakagami, H., Fukaya, M., Watanabe, M., Hatanaka, N., Totsuka, M., Yagi, T., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0707-09.2009 · Cited by 146
Kim, K., Lakhanpal, G., Lu, H. E., Khan, M., Suzuki, A., Kato Hayashi, M., Narayanan, R., Luyben, T. T., Matsuda, T., Nagai, T., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.07.023 · Cited by 145
Self-citationA central role for the small GTPase Rac1 in hippocampal plasticity and spatial learning and memory
Haditsch, U., Leone, D. P., Farinelli, M., Chrostek‐Grashoff, A., Brakebusch, C., Mansuy, I. M., McConnell, S. K., & Palmer, T. D. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.04.005 · Cited by 144
Murakoshi, H., Shin, M. E., Parra-Bueno, P., Szatmari, E. M., Shibata, A. C. E., & Yasuda, R. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.036 · Cited by 140
Self-citationAlev, C., Urschel, S., Sonntag, S., Zoidl, G., Fort, A., Höher, T., Matsubara, M., Willecke, K., Spray, D. C., & Dermietzel, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805408105 · Cited by 128
Convergent CaMK and RacGEF signals control dendritic structure and function
Penzes, P., Cahill, M. E., Jones, K. A., & Srivastava, D. P. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.07.002 · Cited by 123
Intersubunit capture of regulatory segments is a component of cooperative CaMKII activation
Chao, L. H., Pellicena, P., Deindl, S., Barclay, L. A., Schulman, H., & Kuriyan, J. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1751 · Cited by 119
Bhattacharyya, M., Stratton, M. M., Going, C. C., McSpadden, E. D., Huang, Y., Susa, A. C., Elleman, A., Cao, Y. M., Pappireddi, N., Burkhardt, P., et al. (2016) · eLife · doi:10.7554/elife.13405 · Cited by 112
Self-citationRac1 Induces the Clustering of AMPA Receptors during Spinogenesis
Wiens, K. M., Lin, H., & Liao, D. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1947-05.2005 · Cited by 111
Ma, X., Wang, Y., Ferraro, F., Mains, R. E., & Eipper, B. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5283-07.2008 · Cited by 102
The eag Potassium Channel Binds and Locally Activates Calcium/Calmodulin-dependent Protein Kinase II
Sun, X. X., Hodge, J. J. L., Zhou, Y., Nguyen, M.-D., & Griffith, L. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310728200 · Cited by 98
Kalirin and Trio proteins serve critical roles in excitatory synaptic transmission and LTP
Herring, B. E., & Nicoll, R. A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600179113 · Cited by 98
Saneyoshi, T., & Hayashi, Y. (2012) · Cytoskeleton · doi:10.1002/cm.21037 · Cited by 83
Self-citationDynamic Control of Excitatory Synapse Development by a Rac1 GEF/GAP Regulatory Complex
Um, K., Niu, S., Duman, J. G., Cheng, J. X., Tu, Y.-K., Schwechter, B., Liu, F., Hiles, L., Narayanan, A. S., Ash, R. T., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.05.011 · Cited by 81
Stabilization of Calmodulin-dependent Protein Kinase II through the Autoinhibitory Domain (*)
Ishida, A., & Fujisawa, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.5.2163 · Cited by 77
Stoichiometry and Phosphoisotypes of Hippocampal AMPA-Type Glutamate Receptor Phosphorylation
Hosokawa, T., Mitsushima, D., Kaneko, R., & Hayashi, Y. (2014) · Neuron · doi:10.1016/j.neuron.2014.11.026 · Cited by 66
Self-citationMizutani, A., Kuroda, Y., Futatsugi, A., Furuichi, T., & Mikoshiba, K. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4738-07.2008 · Cited by 65
Criteria for identifying the molecular basis of the engram (CaMKII, PKMzeta)
Lisman, J. E. (2017) · Molecular Brain · doi:10.1186/s13041-017-0337-4 · Cited by 64
Noguchi, J., Hayama, T., Watanabe, S., Ucar, H., Yagishita, S., Takahashi, N., & Kasai, H. (2016) · Scientific Reports · doi:10.1038/srep32897 · Cited by 60 · cited 1×
“One of the final effectors of Rac1 is cofilin, which rapidly and persistently ( 1 h) accumulates in spines after LTP induction and regulates the dynamics of actin (Bosch et al., 2014; Noguchi et al., 2016).”
Quantitative estimates of the cytoplasmic, PSD, and NMDAR-bound pools of CaMKII in dendritic spines
Feng, B., Raghavachari, S., & Lisman, J. (2011) · Brain Research · doi:10.1016/j.brainres.2011.08.051 · Cited by 46
Improving a Natural CaMKII Inhibitor by Random and Rational Design
Coultrap, S. J., & Bayer, K. U. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025245 · Cited by 43
Genetically encoded probe for fluorescence lifetime imaging of CaMKII activity
Kwok, S., Lee, C., Sánchez, S. A., Hazlett, T. L., Gratton, E., & Hayashi, Y. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.02.070 · Cited by 34
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Murakoshi, H., Eun, S. M., Parra-Bueno, P., Erzsebet, M. S., Akihiro, C. E. S., & Yasuda, R. (2017) · Neuron · Cited by 27
Self-citationIn Vitro Reconstitution of a CaMKII Memory Switch by an NMDA Receptor-Derived Peptide
Urakubo, H., Sato, M., Ishii, S., & Kuroda, S. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.01.026 · Cited by 26
Bhattacharyya, M., Stratton, M. M., Going, C. C., McSpadden, E. D., Huang, Y., Susa, A. C., Elleman, A. V., Cao, Y. M., Pappireddi, N., Burkhardt, P., et al. (2016) · eLife · doi:10.7554/elife.13405.039 · Cited by 2
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Bayer, K. U., & Schulman, H. (2019) · Neuron · doi:10.1016/j.neuron.2019.05.033 · Cited by 314
Spine dynamics in the brain, mental disorders and artificial neural networks
Kasai, H., Ziv, N. E., Okazaki, H., Yagishita, S., & Toyoizumi, T. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00467-3 · Cited by 184
NMDA receptor functions in health and disease: Old actor, new dimensions
Dupuis, J. P., Nicole, O., & Groc, L. (2023) · Neuron · doi:10.1016/j.neuron.2023.05.002 · Cited by 175
CaMKII activation persistently segregates postsynaptic proteins via liquid phase separation
Hosokawa, T., Liu, P.-W., Cai, Q., Ferreira, J. S., Levet, F., Butler, C., Sibarita, J.-B., Choquet, D., Groc, L., Hosy, E., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-021-00843-3 · Cited by 146
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Metadata
- 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
- 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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