The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure
Open accessAbstract
Ca 2+ -calmodulin-dependent protein kinase II (CaMKII) is a serine/threonine protein kinase critically involved in synaptic plasticity in the brain. It is highly concentrated in the postsynaptic density fraction, exceeding the amount of any other signal transduction molecules. Because kinase signaling can be amplified by catalytic reaction, why CaMKII exists in such a large quantity has been a mystery. Here, we provide biochemical evidence that CaMKII is capable of bundling F-actin through a stoichiometric interaction. Consistent with this evidence, in hippocampal neurons, RNAi-mediated down-regulation of CaMKII leads to a reduction in the volume of dendritic spine head that is mediated by F-actin dynamics. An overexpression of CaMKII slowed down the actin turnover in the spine head. This activity was associated with β subunit of CaMKII in a manner requiring its actin-binding and association domains but not the kinase domain. This finding indicates that CaMKII serves as a central signaling molecule in both functional and structural changes during synaptic plasticity.
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Upon activation CaMKIIβ dissociates from F-actin because of competition with Ca2+/CaM for the F-actin binding region, and dissociation is made more persistent by specific autophosphorylation of CaMKIIβ in the F-actin binding region.
“Upon activation CaMKIIβ dissociates from F-actin because of competition with Ca2+/CaM for the F-actin binding region, and dissociation is made more persistent by specific autophosphorylation of CaMKIIβ in the F-actin binding region (171–174).”
From Synaptic memory and CaMKII (2023) · cites this paper as [174]
The Results section, “Activation of CaMKII Leads to a Loss of Bundling Activity” (page not provided), reports that Ca2+/calmodulin activation reverses CaMKIIβ-mediated F-actin bundling and that autophosphorylation contributes to a longer-lasting reversal. It does not establish that Ca2+/calmodulin competes specifically for the F-actin-binding region, or identify specific phosphorylation sites there as the cause of persistent dissociation. (LLM, conf=0.84)
Experimental — accuracy not yet measuredCaMKII is a calcium-activated kinase involved in structural plasticity by remodeling of the postsynaptic density, rearrangement of the actin cytoskeleton and maintenance of spine enlargement.
“CaMKII is a calcium-activated kinase involved in structural plasticity by remodeling of the postsynaptic density (Yoshimura et al., 2002), rearrangement of the actin cytoskeleton (Okamoto et al., 2007) and maintenance of spine enlargement (Matsuzaki et al., 2004; Lee et al., 2009).”
From Barriers in the brain: resolving dendritic spine morphology and compartmentalization (2014) · cites this paper as Okamoto et al., 2007
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Cites
A synaptic model of memory: long-term potentiation in the hippocampus
Bliss, T. V. P., & Collingridge, G. L. (1993) · Nature · doi:10.1038/361031a0 · Cited by 11,566 · see citing works
A Multiple Comparison Procedure for Comparing Several Treatments with a Control
Dunnett, C. W. (1955) · Journal of the American Statistical Association · doi:10.1080/01621459.1955.10501294 · Cited by 5,930 · see citing works
AMPA Receptor Trafficking and Synaptic Plasticity
Malinow, R., & Malenka, R. C. (2002) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.25.112701.142758 · Cited by 2,588 · see citing works
Structural basis of long-term potentiation in single dendritic spines
Matsuzaki, M., Honkura, N., Ellis-Davies, G. C. R., & Kasai, H. (2004) · Nature · doi:10.1038/nature02617 · Cited by 2,500 · see citing works
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 · see citing works
Hayashi, Y., Shi, S.-H., Esteban, J. A., Piccini, A., Poncer, J.-C., & Malinow, R. (2000) · Science · doi:10.1126/science.287.5461.2262 · Cited by 1,524 · see citing works
Self-citationRapid Spine Delivery and Redistribution of AMPA Receptors After Synaptic NMDA Receptor Activation
Shi, S.-H., Hayashi, Y., Petralia, R. S., Zaman, S. H., Wenthold, R. J., Svoboda, K., & Malinow, R. (1999) · Science · doi:10.1126/science.284.5421.1811 · Cited by 1,276 · see citing works
Self-citationMorphological Changes in Dendritic Spines Associated with Long-Term Synaptic Plasticity
Yuste, R., & Bonhoeffer, T. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1071 · Cited by 1,269 · see citing works
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 · see citing works
Structural plasticity and memory
Lamprecht, R., & LeDoux, J. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1301 · Cited by 1,010 · see citing works
Okamoto, K.-I., Nagai, T., Miyawaki, A., & Hayashi, Y. (2004) · Nature Neuroscience · doi:10.1038/nn1311 · Cited by 854 · see citing works
Self-citationDerkach, V., Barria, A., & Soderling, T. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3269 · Cited by 842 · see citing works
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 · see citing works
Shen, K., & Meyer, T. (1999) · Science · doi:10.1126/science.284.5411.162 · Cited by 673 · see citing works
Regional distribution of type II Ca2+/calmodulin-dependent protein kinase in rat brain
Erondu, N., & Kennedy, M. (1985) · The Journal of Neuroscience · doi:10.1523/jneurosci.05-12-03270.1985 · Cited by 630 · see citing works
Butz, S., Okamoto, M., & Südhof, T. C. (1998) · Cell · doi:10.1016/s0092-8674(00)81736-5 · Cited by 548 · see citing works
Modulation of AMPA receptor unitary conductance by synaptic activity
Benke, T. A., Lüthi, A., Isaac, J. T. R., & Collingridge, G. L. (1998) · Nature · doi:10.1038/31709 · Cited by 533 · see citing works
An actin nucleation mechanism mediated by Bni1 and Profilin
Sagot, I., Rodal, A. A., Moseley, J. B., Goode, B. L., & Pellman, D. S. (2002) · Nature Cell Biology · doi:10.1038/ncb834 · Cited by 493 · see citing works
Peng, J., Kim, M. J., Cheng, D., Duong, D. M., Gygi, S. P., & Sheng, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400103200 · Cited by 473 · see citing works
Rapid turnover of actin in dendritic spines and its regulation by activity
Star, E. N., Kwiatkowski, D. J., & Murthy, V. N. (2002) · Nature Neuroscience · doi:10.1038/nn811 · Cited by 465 · see citing works
McGlade-McCulloh, E., Yamamoto, H., Tan, S.-E., Brickey, D. A., & Soderling, T. (1993) · Nature · doi:10.1038/362640a0 · Cited by 441 · see citing works
Synapsin I bundles F-actin in a phosphorylation-dependent manner
Bähler, M., & Greengard, P. (1987) · Nature · doi:10.1038/326704a0 · Cited by 417 · see citing works
Shen, K., Teruel, M. N., Subramanian, K., & Meyer, T. (1998) · Neuron · doi:10.1016/s0896-6273(00)80569-3 · Cited by 350 · see citing works
Fink, C. C., Bayer, K.-U., Myers, J. W., Ferrell, J. E., Schulman, H., & Meyer, T. (2003) · Neuron · doi:10.1016/s0896-6273(03)00428-8 · Cited by 328 · see citing works
Thiagarajan, T. C., Piedras-Renterı́a, E. S., & Tsien, R. W. (2002) · Neuron · doi:10.1016/s0896-6273(02)01049-8 · Cited by 288 · see citing works
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 · see citing works
Dendritic spine geometry: functional implication and regulation
Hayashi, Y., & Majewska, A. K. (2005) · Neuron · doi:10.1016/j.neuron.2005.05.006 · Cited by 237 · see citing works
Self-citationWalikonis, 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 · see citing works
Hudmon, A., LeBel, E., Roy, H., Sik, A., Schulman, H., Waxham, M. N., & De Koninck, P. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4698-04.2005 · Cited by 159 · see citing works
Visualization 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 150 · see citing works
Self-citationRobison, A. J., Bass, M. A., Jiao, Y., MacMillan, L. B., Carmody, L. C., Bartlett, R. K., & Colbran, R. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502191200 · Cited by 134 · see citing works
Dhavan, R., Greer, P. L., Morabito, M. A., Orlando, L. R., & Tsai, L. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-18-07879.2002 · Cited by 116 · see citing works
Capani, F., Martone, M. E., Deerinck, T. J., & Ellisman, M. H. (2001) · The Journal of Comparative Neurology · doi:10.1002/cne.1199 · Cited by 113 · see citing works
CaMKIIβ Association with the Actin Cytoskeleton Is Regulated by Alternative Splicing
O'Leary, H., Lasda, E., & Bayer, K. U. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-03-0252 · Cited by 113 · see citing works
Waxham, M. N., Tsai, A.-L., & Putkey, J. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.28.17579 · Cited by 69 · see citing works
Ohta, Y., Nishida, E., & Sakai, H. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)81061-4 · Cited by 43 · see citing works
Role of β isoform‐specific insertions of Ca2+/calmodulin‐dependent protein kinase II
Urushihara, M., & Yamauchi, T. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02410.x · Cited by 12 · see citing works
Flagged first, then by citations
1 of the 38 references couldn’t be matched to a known paper.
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- [37]Dunnett CW. J Am Stat Assoc. 1955;50:1096–1121. [[Google Scholar](https://scholar.google.com/scholar_lookup?journal=J%20Am%20Stat%20Assoc&author=CW%20Dunnett&volume=50&publication_year=1955&pages=1096-1121&)]
Cited by
Sorted by citations
Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy.
Cingolani, L. A., & Goda, Y. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2373 · Cited by 831 · see citing works
Actin in dendritic spines: connecting dynamics to function
Hotulainen, P., & Hoogenraad, C. C. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003008 · Cited by 815 · see citing works
Making memories last: the synaptic tagging and capture hypothesis
Redondo, R. L., & Morris, R. G. M. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn2963 · Cited by 792 · see citing works
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 · see citing works
Self-citationThe Postsynaptic Organization of Synapses
Sheng, M., & Kim, E. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005678 · Cited by 603 · see citing works
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 · see citing works
Self-citationCalmodulin-kinases: modulators of neuronal development and plasticity.
Wayman, G. A., Lee, Y.-S., Tokumitsu, H., Silva, A., & Soderling, T. R. (2008) · Neuron · doi:10.1016/j.neuron.2008.08.021 · Cited by 567 · see citing works
The Subspine Organization of Actin Fibers Regulates the Structure and Plasticity of Dendritic Spines
Honkura, N., Matsuzaki, M., Noguchi, J., Ellis-Davies, G. C. R., & Kasai, H. (2008) · Neuron · doi:10.1016/j.neuron.2008.01.013 · Cited by 490 · see citing works
Dendritic Spines: The Locus of Structural and Functional Plasticity
Sala, C., & Segal, M. (2014) · Physiological Reviews · doi:10.1152/physrev.00012.2013 · Cited by 465 · see citing works
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 · see citing works
Self-citationβCaMKII in Lateral Habenula Mediates Core Symptoms of Depression
Li, K., Zhou, T., Liao, L., Yang, Z., Wong, C., Henn, F., Malinow, R., Yates, J. R., & Hu, H. (2013) · Science · doi:10.1126/science.1240729 · Cited by 411 · see citing works
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 · see citing works
Self-citationCaMKII Triggers the Diffusional Trapping of Surface AMPARs through Phosphorylation of Stargazin
Opazo, P., Labrecque, S., Tigaret, C. M., Frouin, A., Wiseman, P. W., Koninck, P. D., & Choquet, D. (2010) · Neuron · doi:10.1016/j.neuron.2010.06.007 · Cited by 403 · see citing works
Glutamate receptor dynamics in dendritic microdomains.
Newpher, T. M., & Ehlers, M. D. (2008) · Neuron · doi:10.1016/j.neuron.2008.04.030 · Cited by 356 · see citing works
CaMKII: Claiming Center Stage in Postsynaptic Function and Organization
Hell, J. W. (2014) · Neuron · doi:10.1016/j.neuron.2013.12.024 · Cited by 352 · see citing works
Inverse synaptic tagging of inactive synapses via dynamic interaction of Arc/Arg3.1 with CaMKIIβ
Okuno, H., Akashi, K., Ishii, Y., Yagishita-Kyo, N., Suzuki, K., Nonaka, M., Kawashima, T., Fujii, H., Takemoto-Kimura, S., Abe, M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.02.062 · Cited by 310 · see citing works
CaMKII regulation in information processing and storage
Coultrap, S. J., & Bayer, K. U. (2012) · Trends in Neurosciences · doi:10.1016/j.tins.2012.05.003 · Cited by 313 · see citing works
Autophosphorylated CaMKIIα Acts as a Scaffold to Recruit Proteasomes to Dendritic Spines
Bingol, B., Wang, C.-F., Arnott, D., Cheng, D., Peng, J., & Sheng, M. (2010) · Cell · doi:10.1016/j.cell.2010.01.024 · Cited by 268 · see citing works
Steiner, P., Higley, M. J., Xu, W., Czervionke, B. L., Malenka, R. C., & Sabatini, B. L. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.014 · Cited by 259 · see citing works
Lin, Y., & Koleske, A. J. (2010) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-060909-153204 · Cited by 241 · see citing works
CaMKII 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 · see citing works
Ciani, L., Boyle, K. A., Dickins, E. M., Sahores, M., Anane, D., Lopes, D. M., Gibb, A. J., & Salinas, P. C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018132108 · Cited by 209 · see citing works
Okamoto, K., Bosch, M., & Hayashi, Y. (2009) · Physiology · doi:10.1152/physiol.00029.2009 · Cited by 197 · see citing works
Self-citationCaMKII Isoforms in Learning and Memory: Localization and Function
Zalcman, G., Federman, N., & Romano, A. G. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00445 · Cited by 185 · see citing works
Borovac, J., Bosch, M., & Okamoto, K. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.07.001 · Cited by 181 · see citing works
Self-citationSpine 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 180 · see citing works
Takata, K., Kitamura, Y., Saeki, M., Terada, M., Kagitani, S., Kitamura, R., Fujikawa, Y., Maelicke, A., Tomimoto, H., Taniguchi, T., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.142356 · Cited by 176 · see citing works
Akashi, K., Kakizaki, T., Kamiya, H., Fukaya, M., Yamasaki, M., Abe, M., Natsume, R., Watanabe, M., & Sakimura, K. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.5531-08.2009 · Cited by 163 · see citing works
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 · see citing works
Calmodulin kinases: essential regulators in health and disease
Takemoto‐Kimura, S., Suzuki, K., Horigane, S., Kamijo, S., Inoue, M., Sakamoto, M., Fujii, H., & Bito, H. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14020 · Cited by 171 · see citing works
Postsynaptic signaling during plasticity of dendritic spines
Murakoshi, H., & Yasuda, R. (2012) · Trends in Neurosciences · doi:10.1016/j.tins.2011.12.002 · Cited by 158 · see citing works
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 · see citing works
Self-citationJohnson, H. W., & Schell, M. J. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-01-0083 · Cited by 156 · see citing works
Neuronal Gene Targets of NF-κB and Their Dysregulation in Alzheimer's Disease
Snow, W. M., & Albensi, B. C. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00118 · Cited by 157 · see citing works
Chazeau, A., Mehidi, A., Nair, D. K., Gautier, J. J., Leduc, C., Chamma, I., Kage, F., Kechkar, A., Thoumine, O. R., Rottner, K., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488837 · Cited by 141 · see citing works
Yamagata, 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 · see citing works
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 · see citing works
Self-citationGardoni, F., Mauceri, D., Malinverno, M., Polli, F., Costa, C., Tozzi, A., Siliquini, S., Picconi, B., Cattabeni, F., Calabresi, P., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3921-08.2009 · Cited by 142 · see citing works
The Postsynaptic Density: There Is More than Meets the Eye
Dosemeci, A., Weinberg, R. J., Reese, T. S., & Tao-Cheng, J.-H. (2016) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2016.00023 · Cited by 138 · see citing works
Wang, Q., Symes, A. J., Kane, C. A., Freeman, A., Nariculam, J., Munson, P., Thrasivoulou, C., Masters, J. R., & Ahmed, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010456 · Cited by 136 · see citing works
Shonesy, B. C., Jalan‐Sakrikar, N., Cavener, V. S., & Colbran, R. J. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-420170-5.00003-9 · Cited by 134 · see citing works
Kommaddi, R. P., Das, D., Karunakaran, S., Nanguneri, S., Bapat, D., Ray, A., Shaw, E., Bennett, D. A., Nair, D., & Ravindranath, V. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.2127-17.2017 · Cited by 135 · see citing works
Ramachandran, B., & Frey, J. U. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2045-09.2009 · Cited by 130 · see citing works
LTP-Induced Long-Term Stabilization of Individual Nascent Dendritic Spines
Hill, T. C., & Zito, K. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.1404-12.2013 · Cited by 129 · see citing works
βCaMKII controls the direction of plasticity at parallel fiber–Purkinje cell synapses
van Woerden, G. M., Hoebeek, F. E., Gao, Z., Nagaraja, R. Y., Hoogenraad, C. C., Kushner, S. A., Hansel, C., Zeeuw, C. I. D., & Elgersma, Y. (2009) · Nature Neuroscience · doi:10.1038/nn.2329 · Cited by 132 · see citing works
GKAP orchestrates activity-dependent postsynaptic protein remodeling and homeostatic scaling
Shin, S. M., Zhang, N., Hansen, J., Gerges, N. Z., Pak, D. T. S., Sheng, M., & Lee, S. H. (2012) · Nature Neuroscience · doi:10.1038/nn.3259 · Cited by 126 · see citing works
Self-citationNicoll, R. A., & Schulman, H. (2023) · Physiological Reviews · doi:10.1152/physrev.00034.2022 · Cited by 126 · see citing works
“Upon activation CaMKII b dissociates from F-actin because of competition with Ca 2 1 / CaM for the F-actin binding region, and dissociation is made more persistent by speci fi c autophosphorylation of CaMKII b in the F-actin binding region (171 – 174).”
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Vargas, J., Loría, F., Wu, Y.-J., Córdova, G., Nonaka, T., Bellow, S., Syan, S., Hasegawa, M., van Woerden, G. M., Trollet, C., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018101230 · Cited by 121 · see citing works
Plasticity of dendritic spines: subcompartmentalization of signaling
Colgan, L. A., & Yasuda, R. (2014) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170400 · Cited by 124 · see citing works
Borgesius, N. Z., van Woerden, G. M., Buitendijk, G. H. S., Keijzer, N., Jaarsma, D., Hoogenraad, C. C., & Elgersma, Y. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5105-10.2011 · Cited by 124 · see citing works
Coordination of Protein Phosphorylation and Dephosphorylation in Synaptic Plasticity
Woolfrey, K. M., & Dell’Acqua, M. L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.657262 · Cited by 118 · see citing works
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Pelucchi, S., Stringhi, R., & Marcello, E. E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030908 · Cited by 116 · see citing works
Structural Modulation of Dendritic Spines during Synaptic Plasticity
Fortin, D. A., Srivastava, T., & Soderling, T. R. (2011) · The Neuroscientist · doi:10.1177/1073858411407206 · Cited by 116 · see citing works
Dendritic spine actin dynamics in neuronal maturation and synaptic plasticity
Hlushchenko, I., Koskinen, M., & Hotulainen, P. (2016) · Cytoskeleton · doi:10.1002/cm.21280 · Cited by 109 · see citing works
LTP induction by structural rather than enzymatic functions of CaMKII
Tullis, J. E., Larsen, M. E., Rumian, N. L., Freund, R. K., Boxer, E. E., Brown, C. N., Coultrap, S. J., Schulman, H., Aoto, J., Dell’Acqua, M. L., et al. (2023) · Nature · doi:10.1038/s41586-023-06465-y · Cited by 112 · see citing works
Hayashi, Y. (2022) · Neuroscience Research · doi:10.1016/j.neures.2021.08.001 · Cited by 102 · see citing works
Self-citationStructure and function of dendritic spines within the hippocampus
Halbach, O. V. B. U. (2009) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2009.08.006 · Cited by 99 · see citing works
CaMKIIβ binding to stable F-actin <i>in vivo</i> regulates F-actin filament stability
Lin, Y.-C., & Redmond, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804399105 · Cited by 96 · see citing works
Novel insights into CaMKII function and regulation during memory formation
Lucchesi, W., Mizuno, K., & Giese, K.-P. (2010) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2010.10.009 · Cited by 95 · see citing works
Experience-Dependent Induction of Hippocampal ΔFosB Controls Learning
Eagle, A. L., Gajewski, P. A., Yang, M., Kechner, M., Klump, B. M., Kennedy, P., Wang, H., Mazei‐Robison, M. S., & Robison, A. J. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2083-15.2015 · Cited by 92 · see citing works
Regulation of the Wnt/β-Catenin Signaling Pathway by Human Papillomavirus E6 and E7 Oncoproteins
Muñoz-Bello, J. O., Olmedo‐Nieva, L., Contreras‐Paredes, A., Gonzalez, A., Rocha‐Zavaleta, L., & Lizano, M. (2015) · Viruses · doi:10.3390/v7082842 · Cited by 94 · see citing works
Pi, H. J., Otmakhov, N., Gaamouch, F. E., Lemelin, D., Koninck, P. D., & Lisman, J. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009268107 · Cited by 94 · see citing works
Akita, T., Aoto, K., Kato, M., Shiina, M., Mutoh, H., Nakashima, M., Kuki, I., Okazaki, S., Magara, S., Shiihara, T., et al. (2018) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.528 · Cited by 87 · see citing works
Rostas, J. A. P., & Skelding, K. A. (2023) · Cells · doi:10.3390/cells12030401 · Cited by 85 · see citing works
Organization and dynamics of the actin cytoskeleton during dendritic spine morphological remodeling
Chazeau, A., & Giannone, G. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2214-1 · Cited by 85 · see citing works
Examining Form and Function of Dendritic Spines
Lee, K. F. H., Soares, C., & Béïque, J.-C. (2012) · Neural Plasticity · doi:10.1155/2012/704103 · Cited by 82 · see citing works
Tagawa, K., Homma, H., Saito, A., Fujita, K., Chen, X., Imoto, S., Oka, T., Ito, H., Motoki, K., Yoshida, C., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddu475 · Cited by 86 · see citing works
Regulation of dendrite morphogenesis by extrinsic cues
Valnegri, P., Puram, S. V., & Bonni, A. (2015) · Trends in Neurosciences · doi:10.1016/j.tins.2015.05.003 · Cited by 75 · see citing works
Saneyoshi, T., & Hayashi, Y. (2012) · Cytoskeleton · doi:10.1002/cm.21037 · Cited by 78 · see citing works
Self-citationLu, H. E., MacGillavry, H. D., Frost, N. A., & Blanpied, T. A. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.4364-13.2014 · Cited by 78 · see citing works
Sajikumar, S., Li, Q., Abraham, W. C., & Xiao, Z. (2009) · Learning & Memory · doi:10.1101/lm.1255909 · Cited by 78 · see citing works
Ephrin-A5 and EphA5 Interaction Induces Synaptogenesis during Early Hippocampal Development
Akaneya, Y., Sohya, K., Kitamura, A., Kimura, F., Washburn, C. P., Zhou, R., Ninan, I., Tsumoto, T., & Ziff, E. B. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012486 · Cited by 77 · see citing works
Hoffman, L., Farley, M. M., & Waxham, M. N. (2013) · Biochemistry · doi:10.1021/bi3016586 · Cited by 76 · see citing works
βCaMKII Regulates Actin Assembly and Structure
Sanabria, H., Swulius, M. T., Kolodziej, S. J., Liu, J., & Waxham, M. N. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809518200 · Cited by 75 · see citing works
The structure and function of actin cytoskeleton in mature glutamatergic dendritic spines
Bellot, A., Guivernau, B., Tajes, M., Bosch-Morató, M., Valls-Comamala, V., & Muñoz, F. J. (2014) · Brain Research · doi:10.1016/j.brainres.2014.05.024 · Cited by 74 · see citing works
Control of Synapse Structure and Function by Actin and Its Regulators
Gentile, J. E., Carrizales, M. G., & Koleske, A. J. (2022) · Cells · doi:10.3390/cells11040603 · Cited by 67 · see citing works
Zheng, H., Chu, J., Zeng, Y., Loh, H. H., & Law, P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.112607 · Cited by 74 · see citing works
Baucum, A. J., Shonesy, B. C., Rose, K. L., & Colbran, R. J. (2015) · ACS Chemical Neuroscience · doi:10.1021/cn500337u · Cited by 71 · see citing works
Initial 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 71 · see citing works
Interaction Between CaMKII and GluN2B Controls ERK-Dependent Plasticity
Gaamouch, F. E., Buisson, A., Moustié, O., Lemieux, M., Labrecque, S., Bontempi, B., Koninck, P. D., & Nicole, O. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5622-11.2012 · Cited by 73 · see citing works
A CaMKIIβ signaling pathway at the centrosome regulates dendrite patterning in the brain
Puram, S. V., Kim, A. H., Ikeuchi, Y., Wilson‐Grady, J., Merdes, A., Gygi, S. P., & Bonni, A. (2011) · Nature Neuroscience · doi:10.1038/nn.2857 · Cited by 71 · see citing works
Kielland, A., Bochorishvili, G., Corson, J. A., Zhang, L., Rosin, D. L., Heggelund, P., & Zhu, J. (2009) · Neuron · doi:10.1016/j.neuron.2009.03.001 · Cited by 68 · see citing works
Kukushkin, N. V., & Carew, T. J. (2017) · Neuron · doi:10.1016/j.neuron.2017.05.029 · Cited by 68 · see citing works
Takata, K., Amamiya, T., Mizoguchi, H., Kawanishi, S., Kuroda, E., Kitamura, R., Ito, A., Saito, Y., Tawa, M., Nagasawa, T., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.10.021 · Cited by 67 · see citing works
A network of networks: cytoskeletal control of compartmentalized function within dendritic spines
Frost, N. A., Kerr, J. M., Lu, H. E., & Blanpied, T. A. (2010) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2010.06.009 · Cited by 65 · see citing works
Dendritic spine actin cytoskeleton in autism spectrum disorder
Joensuu, M., Lanoue, V., & Hotulainen, P. (2018) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2017.08.023 · Cited by 65 · see citing works
Cohen, H., Kozlovsky, N., Matar, M. A., Zohar, J., & Kaplan, Z. (2014) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2014.09.009 · Cited by 63 · see citing works
Barriers in the brain: resolving dendritic spine morphology and compartmentalization
Adrian, M., Kusters, R., Wierenga, C. J., Storm, C., Hoogenraad, C. C., & Kapitein, L. C. (2014) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2014.00142 · Cited by 62 · see citing works
“This means that voltage signals from the dendrite propagate without attenuation into the spines (Holthoff et al., 2010; Carter et al., 2012; Popovic et al., 2014), but synaptic potentials generated inside the spine head are filtered when they travel to the dendrite (Araya et al., 2006, 2014; Harnett et al., 2012).”
InfluentialYamada, H., Abe, T., Satoh, A., Okazaki, N., Tago, S., Kobayashi, K., Yoshida, Y., Oda, Y., Watanabe, M., Tomizawa, K., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2762-12.2013 · Cited by 62 · see citing works
Kalinowska, M., Chávez, A. E., Lutzu, S., Castillo, P. E., Bukauskas, F. F., & Francesconi, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.640136 · Cited by 57 · see citing works
CaMKIIβ in Neuronal Development and Plasticity: An Emerging Candidate in Brain Diseases
Nicole, O., & Pacary, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197272 · Cited by 60 · see citing works
Woolfrey, K. M., O’Leary, H., Goodell, D. J., Robertson, H. R., Horne, E. A., Coultrap, S. J., Dell’Acqua, M. L., & Bayer, K. U. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.813808 · Cited by 56 · see citing works
Paradoxical signaling regulates structural plasticity in dendritic spines
Rangamani, P., Levy, M. G., Khan, S., & OSTER, G. F. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610391113 · Cited by 51 · see citing works
CaMKII Regulates Oligodendrocyte Maturation and CNS Myelination
Waggener, C. T., Dupree, J. L., Elgersma, Y., & Fuss, B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5875-12.2013 · Cited by 54 · see citing works
Cook, S. G., Bourke, A. M., O’Leary, H., Zaegel, V., Lasda, E. L., Mize-Berge, J., Quillinan, N., Tucker, C. L., Coultrap, S. J., Herson, P. S., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-23779-4 · Cited by 54 · see citing works
Heterogeneity in human hippocampal CaMKII transcripts reveals allosteric hub-dependent regulation
Sloutsky, R., Dziedzic, N., Dunn, M. J., Bates, R. M., Torres‐Ocampo, A. P., Boopathy, S., Page, B., Weeks, J. G., Chao, L. H., & Stratton, M. M. (2020) · Science Signaling · doi:10.1126/scisignal.aaz0240 · Cited by 51 · see citing works
Caldendrin Directly Couples Postsynaptic Calcium Signals to Actin Remodeling in Dendritic Spines
Mikhaylova, M., Bär, J., van Bommel, B., Schätzle, P., Yuanxiang, P., Raman, R., Hradsky, J., Konietzny, A., Loktionov, E. Y., Reddy, P. P., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.01.046 · Cited by 49 · see citing works
Nikandrova, Y., Jiao, Y., Baucum, A. J., Tavalin, S. J., & Colbran, R. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.033985 · Cited by 53 · see citing works
Interplay of enzymatic and structural functions of Ca MKII in long‐term potentiation
Kim, K., Saneyoshi, T., Hosokawa, T., Okamoto, K., & Hayashi, Y. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13672 · Cited by 51 · see citing works
Self-citationBiochemical principles underlying the stable maintenance of LTP by the CaMKII/NMDAR complex
Lisman, J. E., & Raghavachari, S. (2014) · Brain Research · doi:10.1016/j.brainres.2014.12.010 · Cited by 51 · see citing works
- Authors
- Okamoto, K.-I., Narayanan, R., Lee, S. H., Murata, K., & Hayashi, Y.
- Affiliations
- *RIKEN-MIT Neuroscience Research Center, The Picower Institute for Learning and Memory, Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139;
- Massachusetts Institute of Technology (US)
- Medical College of Wisconsin (US)
- Corresponding author
- Hayashi, Yasunori
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-04-10
- Volume
- 104
- Issue
- 15
- Pages
- 6418-6423
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1851051
- OpenAlex
- W2170201765
- Cited by
- 328
- References
- 38
- Citations by year
- 2026: 13 · 2025: 14 · 2024: 12 · 2023: 20 · 2022: 10 · 2021: 13 · 2020: 14 · 2019: 18 · 2018: 20 · 2017: 16 · 2016: 14 · 2015: 19 · 2014: 29 · 2013: 17 · 2012: 20
- FWCI
- 8.49
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ellison Medical Foundation
- National Institutes of Health
- RIKEN
- National Institute on Drug Abuse (R01DA017310)
- 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
- CaMKII, F-actin bundling, synaptic plasticity, postsynaptic density, actin turnover, beta subunit, actin-binding domain, hippocampal neurons
- MeSH terms
- Actins, Animals, Hippocampus, Microscopy, Electron, Scanning, Models, Biological, Neuronal Plasticity, Synapses, Signal Transduction, Calcium-Calmodulin-Dependent Protein Kinases, RNA Interference, Dendritic Spines, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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