The DOI matches its Crossref record; 66 of the 67 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“CaMKII, in turn, phosphorylates Tiam1.”
From Synaptic memory and CaMKII (2023) · cites this paper as [314]
The cited source says what the claim attributes to it.
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Flagged first, then by citations
1 of the 67 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
CaMKII: a central molecular organizer of synaptic plasticity, learning and memory
Yasuda, R., Hayashi, Y., & Hell, J. W. (2022) · Nature Reviews Neuroscience · doi:10.1038/s41583-022-00624-2 · Cited by 431
Self-citationCaM Kinase: Still Inspiring at 40
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
Self-citationNicoll, R. A., & Schulman, H. (2023) · Physiological Reviews · doi:10.1152/physrev.00034.2022 · Cited by 126
“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).”
BackgroundHayashi, Y. (2022) · Neuroscience Research · doi:10.1016/j.neures.2021.08.001 · Cited by 102
Self-citationCaMKIIα-driven, phosphatase-checked postsynaptic plasticity via phase separation
Cai, Q., Zeng, M., Wu, X., Wu, H., Zhan, Y., Tian, R., & Zhang, M. (2021) · Cell Research · doi:10.1038/s41422-020-00439-9 · Cited by 83
Photoactivatable CaMKII induces synaptic plasticity in single synapses
Shibata, A. C. E., Ueda, H. H., Eto, K., Onda, M., Sato, A., Ohba, T., Nabekura, J., & Murakoshi, H. (2021) · Nature Communications · doi:10.1038/s41467-021-21025-6 · Cited by 74
Self-citationCaMKII binds both substrates and activators at the active site
Özden, C., Sloutsky, R., Mitsugi, T., Santos, N., Agnello, E., Gaubitz, C., Foster, J., Lapinskas, E., Esposito, E. A., Saneyoshi, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111064 · Cited by 61
Self-citationInitial memory consolidation and the synaptic tagging and capture hypothesis
Okuda, K., Højgaard, K., Privitera, L., Bayraktar, G., & Takeuchi, T. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14902 · Cited by 74
Non-ionotropic NMDA receptor signaling gates bidirectional structural plasticity of dendritic spines
Stein, I. S., Park, D. K., Claiborne, N., & Zito, K. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108664 · Cited by 69
Meta-reinforcement learning via orbitofrontal cortex
Hattori, R., Hedrick, N. G., Jain, A., Chen, S., You, H., Hattori, M., Choi, J., Lim, B. K., Yasuda, R., & Komiyama, T. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01485-3 · Cited by 75
Self-citationNeuronal ensemble-specific DNA methylation strengthens engram stability
Karaca, K. G., Kupke, J., Brito, D. V. C., Zeuch, B., Thome, C., Weichenhan, D., Lutsik, P., Plass, C., & Oliveira, A. M. M. (2020) · Nature Communications · doi:10.1038/s41467-020-14498-4 · Cited by 74
Ru, Q., Lu, Y., Saifullah, A. B., Blanco, F. A., Yao, C., Cata, J. P., Li, D., Tolias, K. F., & Li, L. (2022) · Journal of Clinical Investigation · doi:10.1172/jci158545 · Cited by 67
The Role of Rac GTPase in Dendritic Spine Morphogenesis and Memory
Costa, J. F., Dines, M., & Lamprecht, R. (2020) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2020.00012 · Cited by 58
Mohanan, A. G., Gunasekaran, S., Jacob, R. S., & Omkumar, R. V. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.855752 · Cited by 55
Yang, Y., & Liu, J. (2022) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2022.102534 · Cited by 49
Li, L., Ru, Q., Lu, Y., Fang, X., Chen, G., Saifullah, A. B., Yao, C., & Tolias, K. F. (2023) · Neuron · doi:10.1016/j.neuron.2023.04.010 · Cited by 44
A revised view of the role of CaMKII in learning and memory
Bayer, K. U., & Giese, K.-P. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01809-x · Cited by 51
Studying CaMKII: Tools and standards
Brown, C. N., & Bayer, K. U. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113982 · Cited by 39
Liaci, C., Camera, M., Caslini, G., Rando, S., Contino, S., Romano, V., & Merlo, G. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116167 · Cited by 40
Okabe, S. (2020) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2020.103564 · Cited by 42
The role of CaMKII autophosphorylation for NMDA receptor-dependent synaptic potentiation
Giese, K.-P. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108616 · Cited by 38
Mechanical regulation of synapse formation and plasticity
Minegishi, T., Kastian, R. F., & Inagaki, N. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.05.017 · Cited by 39
Rac1 is a downstream effector of PKCα in structural synaptic plasticity
Tu, X., Yasuda, R., & Colgan, L. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-58610-6 · Cited by 31
Self-citationRac-maninoff and Rho-vel: The symphony of Rho-GTPase signaling at excitatory synapses
Duman, J. G., Blanco, F. A., Cronkite, C. A., Ru, Q., Erikson, K., Mulherkar, S. A., Saifullah, A. B., Firozi, K., & Tolias, K. F. (2021) · Small GTPases · doi:10.1080/21541248.2021.1885264 · Cited by 35
Tiam1 is Critical for Glutamatergic Synapse Structure and Function in the Hippocampus
Rao, S., Kay, Y., & Herring, B. E. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.1566-19.2019 · Cited by 35
Liu, P.-W., Hosokawa, T., & Hayashi, Y. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.02.004 · Cited by 32
Self-citationGu, H., Zhu, Y., Yang, J., Jiang, R., Deng, Y., Li, A., Fang, Y., Wu, Q., Tu, H., Chang, H., et al. (2023) · Advanced Science · doi:10.1002/advs.202302136 · Cited by 29
Espadas, I., Wingfield, J. L., Nakahata, Y., Chanda, K., Grinman, E., Ghosh, I., Bauer, K. E., Raveendra, B., Kiebler, M. A., Yasuda, R., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46972-8 · Cited by 28
Self-citationRole of calcium/calmodulin-dependent kinase 2 in neurodevelopmental disorders
Onori, M. P., & van Woerden, G. M. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.03.014 · Cited by 30
Imaging dendritic spines: molecular organization and signaling for plasticity
Suratkal, S. S., Yen, Y., & Nishiyama, J. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2020.08.006 · Cited by 30
Cai, Q., Hosokawa, T., Zeng, M., Hayashi, Y., & Zhang, M. (2019) · Structure · doi:10.1016/j.str.2019.11.018 · Cited by 26
Self-citationThe role of CaMKII-Tiam1 complex on learning and memory
Kojima, H., Rosendale, M., Sugiyama, Y., Hayashi, M. K., Horiguchi, Y., Yoshihara, T., Ikegaya, Y., Saneyoshi, T., & Hayashi, Y. (2019) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2019.107070 · Cited by 24
Self-citationMechanical transmission at spine synapses: Short-term potentiation and working memory
Kasai, H., Ucar, H., Morimoto, Y., Eto, F., & Okazaki, H. (2023) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2023.102706 · Cited by 23
Endophilin A1 drives acute structural plasticity of dendritic spines in response to Ca2+/calmodulin
Yang, Y., Jiang, C., Chen, X., Li, D., He, J., Wang, S., Zhao, S. S., Yang, X., Deng, S., Tong, C., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202007172 · Cited by 24
The role of molecular diffusion within dendritic spines in synaptic function
Obashi, K., Taraska, J. W., & Okabe, S. (2021) · The Journal of General Physiology · doi:10.1085/jgp.202012814 · Cited by 24
Single Synapse LTP: A Matter of Context?
Kruijssen, D. L. H., & Wierenga, C. J. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00496 · Cited by 26
Kasai, H. (2023) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.99.018 · Cited by 25
O'Brien, B., Singer, H. A., Adam, A. P., & Ginnan, R. G. (2021) · The FASEB Journal · doi:10.1096/fj.202002755r · Cited by 21
Tebar, F., Chavero, A., Agell, N., Lu, A., Rentero, C., Enrich, C., & Grewal, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103680 · Cited by 21
Kastian, R. F., Minegishi, T., Baba, K., Saneyoshi, T., Katsuno‐Kambe, H., Saranpal, S., Hayashi, Y., & Inagaki, N. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109130 · Cited by 17
Self-citationEngineering memory with an extrinsically disordered kinase
Ripoli, C., Dağliyan, O., Renna, P., Pastore, F., Paciello, F., Sollazzo, R., Rinaudo, M., Battistoni, M., Martini, S., Tramutola, A., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh1110 · Cited by 17
Self-citationCurtis, A. J., Zhu, J., Penny, C. J., & Gold, M. G. (2023) · eLife · doi:10.7554/elife.85008 · Cited by 15
Benson, C. A., Olson, K., Patwa, S., Reimer, M. L., Bangalore, L., Hill, M., Waxman, S. G., & Tan, A. M. (2021) · Scientific Reports · doi:10.1038/s41598-021-87476-5 · Cited by 14
Roles of Rac1-Dependent Intrinsic Forgetting in Memory-Related Brain Disorders: Demon or Angel
Wang, W., Wang, Z., Cao, J., Dong, Y., & Chen, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310736 · Cited by 14
A Lipid-Raft Theory of Alzheimer's Disease
Rappoport, A. (2024) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052024-115455 · Cited by 15
Multiphasic protein condensation governed by shape and valency
Pandey, V., Hosokawa, T., Hayashi, Y., & Urakubo, H. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115504 · Cited by 14
Self-citationPalmitoylated Proteins in Dendritic Spine Remodeling
Albanesi, J. P., Baryłko, B., Demartino, G., & Jameson, D. M. (2020) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2020.00022 · Cited by 13
Vallejo, D., Lindsay, C., González-Billault, C., & Inestrosa, N. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15448 · Cited by 10
Ueda, H. H., Nagasawa, Y., & Murakoshi, H. (2021) · Neuroscience Research · doi:10.1016/j.neures.2021.10.004 · Cited by 12
Self-citationDendritic Spines and Pain Memory
Benson, C. A., King, J. F., Reimer, M. L., Kauer, S. D., Waxman, S. G., & Tan, A. M. (2022) · The Neuroscientist · doi:10.1177/10738584221138251 · Cited by 13
Kaizuka, T., Hirouchi, T., Saneyoshi, T., Shirafuji, T., Collins, M. O., Grant, S. G. N., Hayashi, Y., & Takumi, T. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002006 · Cited by 12
Self-citationAlteration of synaptic protein composition during developmental synapse maturation
Kaizuka, T., & Takumi, T. (2024) · European Journal of Neuroscience · doi:10.1111/ejn.16304 · Cited by 13
Smolen, P. D., Baxter, D. A., & Byrne, J. H. (2020) · Frontiers in Computational Neuroscience · doi:10.3389/fncom.2020.569349 · Cited by 9
Mikuni, T., & Uchigashima, M. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14734 · Cited by 11
Ueda, H. H., Nagasawa, Y., Sato, A., Onda, M., & Murakoshi, H. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110153 · Cited by 11
Self-citationCastillo‐Armengol, J., Marzetta, F., Sánchez-Archidona, A. R., Fledelius, C., Evans, M. L., McNeilly, A. D., McCrimmon, R. J., Ibberson, M. R., & Thorens, B. (2023) · Diabetologia · doi:10.1007/s00125-023-06043-x · Cited by 11
Saneyoshi, T. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.01.018 · Cited by 9
Self-citationLiu, X., & Wang, J. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.07.017 · Cited by 10
Yang, X., Ma, X., Zhao, T., Croucher, D. R., Nguyen, E. V., Clark, K. C., Hu, C., Latham, S. L., Bayly-Jones, C., Nguyen, B. V., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57046-8 · Cited by 9
Self-citationLoss of the polarity protein Par3 promotes dendritic spine neoteny and enhances learning and memory
Voglewede, M. M., Ozsen, E. N., Ivak, N. A., Bernabucci, M., Tang, R., Sun, M., Pang, Z. P., & Zhang, H. (2024) · iScience · doi:10.1016/j.isci.2024.110308 · Cited by 8
Cui, D., Jiang, X., Chen, M., Huan, S., Shao, D., Yang, L. C., Guo, X., Wang, Y., Lai, B., & Zheng, P. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.720371 · Cited by 9
Wang, X.-Z., Wen, L., Zhou, Y., Huang, S., Yang, B., Cheng, S., Zeng, W., Mei, M., Sun, J., Jiang, X. J., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011166 · Cited by 9
MARCKS and PI(4,5)P2 reciprocally regulate actin-based dendritic spine morphology
Calabrese, B., & Halpain, S. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-09-0370 · Cited by 8
Funahashi, Y., Ahammad, R. U., Zhang, X., Hossen, E., Kawatani, M., Nakamuta, S., Yoshimi, A., Wu, M., Wang, H., Wu, M., et al. (2024) · Science Signaling · doi:10.1126/scisignal.ado9852 · Cited by 9
Activity-Dependent Stabilization of Nascent Dendritic Spines Requires Nonenzymatic CaMKIIα Function
Claiborne, N., Anisimova, M., & Zito, K. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1393-22.2023 · Cited by 8
López-García, S., López-Merino, E., Fernández‐Rodrigo, A., Zamorano-González, P., Gutiérrez-Eisman, S., Jiménez-Sánchez, R., & Esteban, J. A. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05394-x · Cited by 5
Liu, S., Qi, R., Zhang, J., Zhang, C., Chen, L., Yao, Z., & Niu, W. (2022) · FEBS Letters · doi:10.1002/1873-3468.14428 · Cited by 5
Regulation of Presynaptic Release Machinery by Cell Adhesion Molecules
Uchigashima, M., Hayashi, Y., & Futai, K. (2023) · Advances in neurobiology · doi:10.1007/978-3-031-34229-5_13 · Cited by 5
Self-citationFujii, H., & Bito, H. (2022) · Neuroscience Research · doi:10.1016/j.neures.2022.04.004 · Cited by 6
The Janus face of CaMKII: from memory consolidation to neurotoxic switch in Alzheimer’s disease
Tang, L., Liu, F., Sun, X., Yang, J., Liu, Y., Pan, X., Hao, L., Lou, F., & Su, J. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04160-7 · Cited by 5
Synaptic Plasticity in the Hippocampus
Bliss, T., Collingridge, G. L., Cooke, S. F., Georgiou, J., & Morris, R. (2025) · Oxford University Press eBooks · doi:10.1093/med/9780190065324.003.0010 · Cited by 4
Presynaptic Rac1 in the hippocampus selectively regulates working memory
Kim, J., Bustamante, E., Sótonyi, P., Maxwell, N. D., Parameswaran, P., Kent, J. K., Wetsel, W. C., Soderblom, E. J., Rácz, B., & Soderling, S. H. (2024) · eLife · doi:10.7554/elife.97289 · Cited by 5
Molecular Underpinnings of Memory Persistence and Forgetting
Dalto, J. F., Medina, J. H., & Pastor, V. E. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70089 · Cited by 4
Synaptic Tagging and Capture: Functional Implications and Molecular Mechanisms
Prodan, A., & Morris, R. (2024) · Springer eBooks · doi:10.1007/978-3-031-54864-2_1 · Cited by 3
LOV2-based photoactivatable CaMKII and its application to single synapses: Local Optogenetics
Nagasawa, Y., Ueda, H. H., Kawabata, H., & Murakoshi, H. (2023) · Biophysics and Physicobiology · doi:10.2142/biophysico.bppb-v20.0027 · Cited by 2
Self-citationSoga, K., Fujiwara, T., Nakagawa, M., Shibata, A., Adriel, H., Yatsuzuka, K., Kakegawa, W., Yuzaki, M., Hamachi, I., Nango, E., et al. (2025) · Science Advances · doi:10.1126/sciadv.adt6683 · Cited by 3
Yamada, S., Yasukuni, R., Bessho, Y., Fujita, Y., Hosokawa, Y., & Matsui, T. (2025) · Nature Communications · doi:10.1038/s41467-025-65474-9 · Cited by 2
Blanco, F. A., Saifullah, A. B., Cheng, J. X., Abella, C., Scala, F., Firozi, K., Niu, S., Park, J., Chin, J., & Tolias, K. F. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.0298-24.2024 · Cited by 2
Activity-dependent regulation of Cdc42 by Ephexin5 drives synapse growth and stabilization
Petshow, S., Coblentz, A., Hamilton, A. M., Sarkar, D., Anisimova, M., Flores, J. C., & Zito, K. (2025) · Science Advances · doi:10.1126/sciadv.adp5782 · Cited by 2
A lipid-raft theory of Alzheimer's disease
Rappoport, A. (2025) · Elsevier eBooks · doi:10.1016/b978-0-44-345008-2.00017-5 · Cited by 2
Costa‐Ferro, Z. S. M., de Oliveira, G. N., da Silva, D. V., Marinowic, D. R., Machado, D. C., Longo, B. M., & da Costa, J. C. (2020) · Brain Structure and Function · doi:10.1007/s00429-020-02159-7 · Cited by 2
Wellendorph, P., Gauger, S. J., Andersen, J. V., Kornum, B. R., Solbak, S. M. Ø., & Frølund, B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100064 · Cited by 2
Yang, K., Zhang, P., Hui, X., Liu, C., Li, J., & Liu, Y. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1718008 · Cited by 1
Zhang, B., Zhang, M., Liu, K., Zhao, C., Zhang, J., Liu, Z., Fan, Y., Gu, R., Lin, L., Fu, C., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117750 · Cited by 2
Ras-related C3 botulinum toxin substrate 1 role in pathophysiology of neurological diseases
Le, N. M., & Li, J. (2022) · Brain Hemorrhages · doi:10.1016/j.hest.2022.05.005 · Cited by 1
Changing the size of dendritic spines
Saneyoshi, T. (2023) · eLife · doi:10.7554/elife.91566 · Cited by 1
Self-citationMolecular Mechanisms Underlying Synaptic Tagging and Consolidation
Hayashi, Y., Bosch, M., Liu, P.-W., Hosokawa, T., & Saneyoshi, T. (2024) · Springer eBooks · doi:10.1007/978-3-031-54864-2_3 · Cited by 1
Self-citationRhoGEF Tiam2 Regulates Glutamatergic Synaptic Transmission in Hippocampal CA1 Pyramidal Neurons
Rao, S., Liang, F., & Herring, B. E. (2024) · eNeuro · doi:10.1523/eneuro.0500-21.2024 · Cited by 1
NMDAR Phosphoproteome Controls Synaptic Growth and LearningPreprint
Funahashi, Y., Ahammad, R. U., Zhang, X., Hossen, E., Kawatani, M., Nakamuta, S., Yoshimi, A., Wu, M., Wang, H., Wu, M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.15.571360 · Cited by 1
Presynaptic Rac1 in the hippocampus selectively regulates working memoryPreprint
Kim, J., Bustamante, E., Sótonyi, P., Maxwell, N. D., Parameswaran, P., Kent, J. K., Wetsel, W. C., Soderblom, E. J., Rácz, B., & Soderling, S. H. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.18.585488 · Cited by 1
Presynaptic Rac1 in the hippocampus selectively regulates working memoryPreprint
Kim, J., Bustamante, E., Sótonyi, P., Maxwell, N. D., Parameswaran, P., Kent, J. K., Wetsel, W. C., Soderblom, E. J., Rácz, B., & Soderling, S. H. (2024) · eLife · doi:10.7554/elife.97289.1 · Cited by 1
Exciting inhibition: Local regulation of synapse formation and plasticity
Kruijssen, D. L. H. (2020) · Utrecht University Repository (Utrecht University) · doi:10.33540/296
CaMKII activation triggers persistent formation and segregation of postsynaptic liquid phase
Liu, P.-W. (2021) · Institutional Repositories DataBase (IRDB) · doi:10.14989/doctor.k23115
Chronic neuronal excitation leads to homeostatic suppression of structural long-term potentiationPreprint
Ueda, H. H., Sato, A., Onda, M., & Murakoshi, H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.16.435575
Self-citationThe Jerusalem Extraterrestrial SpaceshipPreprint
Wolynski, J. J. (2014) · viXra
Calcium | Calcium/Calmodulin-Dependent Protein Kinase II
Hudmon, A., & Schulman, H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00099-2
Increased spine PIP3 is sequestered from dendritic shafts
Ueda, Y., Sugimoto, N., & Ozawa, T. (2022) · Molecular Brain · doi:10.1186/s13041-022-00944-5
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
