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CaMKIIβ Functions As an F-Actin Targeting Module that Localizes CaMKIIα/β Heterooligomers to Dendritic Spines
Open accessAbstract
Ca2+/calmodulin-dependent protein kinase II (CaMKII) is a serine/threonine protein kinase that regulates long-term potentiation and other forms of neuronal plasticity. Functional differences between the neuronal CaMKIIalpha and CaMKIIbeta isoforms are not yet known. Here, we use green fluorescent protein-tagged (GFP-tagged) CaMKII isoforms and show that CaMKIIbeta is bound to F-actin in dendritic spines and cell cortex while CaMKIIalpha is largely a cytosolic enzyme. When expressed together, the two isoforms form large heterooligomers, and a small fraction of CaMKIIbeta is sufficient to dock the predominant CaMKIIalpha to the actin cytoskeleton. Thus, CaMKIIbeta functions as a targeting module that localizes a much larger number of CaMKIIalpha isozymes to synaptic and cytoskeletal sites of action.
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“A second difference is the specific high-affinity binding of the inactive β, but not α, to F-actin (167–170).”
From Synaptic memory and CaMKII (2023) · cites this paper as [168]
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Cites
Control of memory formation through regulated expression of a CaMKII transgene
Mayford, M., Bach, M. E., Huang, Y.-Y., Wang, L., Hawkins, R. D., & Kandel, E. R. (1996) · Science · doi:10.1126/science.274.5293.1678 · Cited by 1,550
Deficient Hippocampal Long-Term Potentiation in α-Calcium-Calmodulin Kinase II Mutant Mice
Silva, A. J., Stevens, C. F., Tonegawa, S., & Wang, Y. (1992) · Science · doi:10.1126/science.1378648 · Cited by 1,472
Sensitivity of CaM Kinase II to the Frequency of Ca 2+ Oscillations
De Koninck, P., & Schulman, H. (1998) · Science · doi:10.1126/science.279.5348.227 · Cited by 1,269
Autophosphorylation at Thr 286 of the α Calcium-Calmodulin Kinase II in LTP and Learning
Giese, K. P., Fedorov, N. B., Filipkowski, R. K., & Silva, A. J. (1998) · Science · doi:10.1126/science.279.5352.870 · Cited by 1,055
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
Rapid Actin-Based Plasticity in Dendritic Spines
Fischer, M., Kaech, S., Knutti, D., & Matus, A. (1998) · Neuron · doi:10.1016/s0896-6273(00)80467-5 · Cited by 905
Evidence for a Role of Dendritic Filopodia in Synaptogenesis and Spine Formation
Ziv, N. E., & Smith, S. J. (1996) · Neuron · doi:10.1016/s0896-6273(00)80283-4 · Cited by 882
Miller, S. (1986) · Cell · doi:10.1016/0092-8674(86)90008-5 · Cited by 864
Contrasting properties of two forms of long-term potentiation in the hippocampus
Nicoll, R. A., & Malenka, R. C. (1995) · Nature · doi:10.1038/377115a0 · Cited by 861
The Multifunctional Calcium/Calmodulin-Dependent Protein Kinase: From Form to Function
Braun, A. P., & Schulman, H. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.002221 · Cited by 820
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Items 101–200 of 349
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 77
Zheng, H., Chu, J., Zeng, Y., Loh, H. H., & Law, P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.112607 · Cited by 75
Baucum, A. J., Shonesy, B. C., Rose, K. L., & Colbran, R. J. (2015) · ACS Chemical Neuroscience · doi:10.1021/cn500337u · Cited by 72
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 74
Cipolletta, E., Monaco, S., Maione, A. S., Vitiello, L., Campiglia, P., Pastore, L., Franchini, C., Novellino, E., Limongelli, V., Bayer, K. U., et al. (2010) · Endocrinology · doi:10.1210/en.2009-1248 · Cited by 73
Schulman, H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3606-04.2004 · Cited by 71
Yao, J., Qi, J., & Chen, G. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1183-06.2006 · Cited by 71
Coullery, R. P., Ferrari, M. E., & Rosso, S. B. (2015) · NeuroToxicology · doi:10.1016/j.neuro.2015.12.004 · Cited by 70
CaMKII, an Enzyme on the Move: Regulation of Temporospatial Localization
Griffith, L. C. (2003) · Molecular Interventions · doi:10.1124/mi.3.7.386 · Cited by 68
Shioda, N., Beppu, H., Fukuda, T., Li, E., Kitajima, I., & Fukunaga, K. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4816-10.2011 · Cited by 69
Kistler, A. D., Singh, G., Altintas, M. M., Yu, H., Fernandez, I. C., Gu, C., Wilson, C., Srivastava, S. K., Dietrich, A., Walz, K., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.488122 · Cited by 66
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 68
Zhang, L., Kirschstein, T., Sommersberg, B., Merkens, M., Manahan‐Vaughan, D., Elgersma, Y., & Beck, H. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2086-05.2005 · Cited by 63
Groth, R. D., Lindskog, M., Thiagarajan, T. C., Li, L., & Tsien, R. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018022108 · Cited by 64
Flexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation
Bhattacharyya, M., Lee, Y. K., Muratcioglu, S., Qiu, B., Nyayapati, P., Schulman, H., Groves, J. T., & Kuriyan, J. (2020) · eLife · doi:10.7554/elife.53670 · Cited by 58
Neural field model of binocular rivalry waves
Bressloff, P. C., & Webber, M. A. (2011) · Journal of Computational Neuroscience · doi:10.1007/s10827-011-0351-y · Cited by 61
Pfleiderer, P. J., Lu, K. K., Crow, M. T., Keller, R. S., & Singer, H. A. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00536.2003 · Cited by 60
Structure and molecular organization of dendritic spines.
Tashiro, A., & Yuste, R. (2003) · PubMed · doi:10.14670/hh-18.617 · Cited by 60
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 65
Grossman, S. D., Futter, M., Snyder, G. L., Allen, P. B., Nairn, A. C., Greengard, P., & Hsieh‐Wilson, L. C. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02491.x · Cited by 62
Diazepam‐induced adaptive plasticity revealed by α1 GABAA receptor‐specific expression profiling
Huopaniemi, L., Keist, R., Randolph, A., Certa, U., & Rudolph, U. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02216.x · Cited by 58
Transcriptional Changes Common to Human Cocaine, Cannabis and Phencyclidine Abuse
Lehrmann, E., Colantuoni, C., Deep‐Soboslay, A., Becker, K. G., Lowe, R. H., Huestis, M. A., Hyde, T. M., Kleinman, J. E., & Freed, W. J. (2006) · PLoS ONE · doi:10.1371/journal.pone.0000114 · Cited by 60
Takeuchi, Y., Yamamoto, H., Fukunaga, K., Miyakawa, T., & Miyamoto, E. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0742557.x · Cited by 58
Easley, C. A., Brown, C. M., Horwitz, A. F., & Tombes, R. M. (2008) · Cell Motility · doi:10.1002/cm.20294 · Cited by 56
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
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
The lysosomal GPCR-like protein GPR137B regulates Rag and mTORC1 localization and activity
Gan, L., Seki, A., Shen, K., Iyer, H., Han, K., Hayer, A., Wollman, R., Ge, X., Lin, J. R., Dey, G., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0321-6 · Cited by 53
Self-citationLiu, B., & Neufeld, A. H. (2000) · Glia · doi:10.1002/(sici)1098-1136(200004)30:2 · Cited by 178
Biochemical 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 54
Nguyen, T. A., Sarkar, P., Veetil, J. V., Koushik, S. V., & Vogel, S. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038209 · Cited by 52
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
Barbiero, V. S., Giambelli, R., Musazzi, L., Tiraboschi, E., Tardito, D., Pérez, J., Drago, F., Racagni, G., & Popoli, M. (2007) · Neuropsychopharmacology · doi:10.1038/sj.npp.1301378 · Cited by 51
Identification of novel phosphorylation sites on postsynaptic density proteins
Jaffe, H., Vinadé, L., & Döṣemeci, A. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.122 · Cited by 48
Regulation of dendritic growth by calcium and neurotrophin signaling
Dijkhuizen, P. A., & Ghosh, A. (2004) · Progress in brain research · doi:10.1016/s0079-6123(04)47002-2 · Cited by 50
Structure and composition of the postsynaptic density during development
Swulius, M. T., Kubota, Y., Forest, A., & Waxham, M. N. (2010) · The Journal of Comparative Neurology · doi:10.1002/cne.22451 · Cited by 51
Wang, Q., Chen, M., Schafer, N. P., Bueno, C., Song, S. S., Hudmon, A., Wolynes, P. G., Waxham, M. N., & Cheung, M. S. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911452116 · Cited by 49
Wang, C.-C., Su, K., Chen, H., Chang, S.-Y., Shen, C.-F., Hsieh, C.-H., Hong, Q.-S., Chiang, C.-C., Chang, G., Yu, S., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124191 · Cited by 48
Toscano, C. D., O'Callaghan, J. P., & Guilarte, T. R. (2005) · Brain Research · doi:10.1016/j.brainres.2005.02.076 · Cited by 48
Chang, H., Minahan, K., Merriman, J. A., & Jones, K. T. (2009) · Development · doi:10.1242/dev.042143 · Cited by 47
Hudmon, A., Kim, S. A., Kolb, S. J., Stoops, J. K., & Waxham, M. N. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00119.x · Cited by 46
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
Identification of two persistently activated neurotrophin-regulated pathways in rat hippocampus
Blanquet, P. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00489-3 · Cited by 47
Assembly of signaling machinery at the postsynaptic membrane
Kirsch, J. (1999) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(99)80048-8 · Cited by 45
Dendritic spine plasticity in hippocampus
Gazzaley, A. H., Kay, S., & Benson, D. L. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00021-0 · Cited by 45
Substrate-selective and Calcium-independent Activation of CaMKII by α-Actinin
Jalan‐Sakrikar, N., Bartlett, R. K., Baucum, A. J., & Colbran, R. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.351817 · Cited by 47
Cytosolic Targeting Domains of γ and δ Calmodulin-dependent Protein Kinase II
Caran, N., Johnson, L. D., Jenkins, K. J., & Tombes, R. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103013200 · Cited by 43
Sugawara, T., Hisatsune, C., Miyamoto, H., Ogawa, N., & Mikoshiba, K. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617270114 · Cited by 45
Dzhura, I., Wu, Y., Colbran, R. J., Corbin, J. D., Balser, J. R., & Anderson, M. E. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.021881 · Cited by 42
RetractedJiao, Y., Jalan‐Sakrikar, N., Robison, A. J., Baucum, A. J., Bass, M. A., & Colbran, R. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.216010 · Cited by 41
Serotonin receptor 1A modulates actin dynamics and restricts dendritic growth in hippocampal neurons
Ferreira, T., Iacono, L. L., & Gross, C. T. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07283.x · Cited by 43
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
Actin and Actin-Binding Proteins: Masters of Dendritic Spine Formation, Morphology, and Function
Lin, W., & Webb, D. J. (2009) · The Open Neuroscience Journal · doi:10.2174/1874082000903020054 · Cited by 42
Activity-dependent redistribution of CaMKII in the postsynaptic compartment of hippocampal neurons
Tao-Cheng, J.-H. (2020) · Molecular Brain · doi:10.1186/s13041-020-00594-5 · Cited by 38
Phase separation-mediated actin bundling by the postsynaptic density condensates
Chen, X., Jia, B., Zhu, S., & Zhang, M. (2023) · eLife · doi:10.7554/elife.84446 · Cited by 39
Regulation of CaMKII In vivo: The Importance of Targeting and the Intracellular Microenvironment
Skelding, K. A., & Rostas, J. A. P. (2009) · Neurochemical Research · doi:10.1007/s11064-009-9985-9 · Cited by 37
Calcium in Cell-Extracellular Matrix Interactions
Gopal, S., Multhaupt, H. A. B., & Couchman, J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-12457-1_43 · Cited by 38
Novak, G., & Seeman, P. (2010) · Synapse · doi:10.1002/syn.20786 · Cited by 37
CaMKII regulates intracellular Ca2+ dynamics in native endothelial cells
Toussaint, F., Charbel, C., Blanchette, A., & Ledoux, J. (2015) · Cell Calcium · doi:10.1016/j.ceca.2015.06.005 · Cited by 36
Ganglioside/calmodulin kinase ii signal inducing cdc42-mediated neuronal actin reorganization
Chen, N., Furuya, S., Doi, H., Hashimoto, Y., Kudo, Y., & Higashi, H. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00259-8 · Cited by 35
Musazzi, L., Daniel, E. D., Maycox, P. R., Racagni, G., & Popoli, M. (2010) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145710001240 · Cited by 36
Gu, Z., Jiang, Q., Yuen, E. Y., & Yan, Z. (2006) · Molecular Pharmacology · doi:10.1124/mol.105.018853 · Cited by 35
Distinct roles of multiple isoforms of CaMKII in signaling to the nucleus
Ma, H., Li, B., & Tsien, R. W. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.02.008 · Cited by 35
Calcium-Associated Proteins in Neuroregeneration
Lisek, M., Tomczak, J., Boczek, T., & Żylińska, L. (2024) · Biomolecules · doi:10.3390/biom14020183 · Cited by 35
Yu, Z., Wu, Y., Wang, Y., Liu, D.-S., Song, X.-L., Jiang, Q., Li, Y., Zhang, S., Xu, N., Zhu, M. X., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aar4481 · Cited by 34
Kool, M. J., van de Bree, J. E., Bodde, H. E., Elgersma, Y., & van Woerden, G. M. (2016) · Scientific Reports · doi:10.1038/srep26989 · Cited by 31
Laminin activates CaMK-II to stabilize nascent embryonic axons
Easley, C. A., Faison, M. O., Kirsch, T. L., Lee, J. A., Seward, M. E., & Tombes, R. M. (2006) · Brain Research · doi:10.1016/j.brainres.2006.03.099 · Cited by 34
Protein targeting and calcium signaling microdomains in neuronal cells
Blackstone, C. D., & Sheng, M. (1999) · Cell Calcium · doi:10.1054/ceca.1999.0071 · Cited by 34
Multiple CaMKII Binding Modes to the Actin Cytoskeleton Revealed by Single-Molecule Imaging
Khan, S., Conte, I. L., Carter, T. D., Bayer, K. U., & Molloy, J. E. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.06.007 · Cited by 31
Mechanisms for localising calcineurin and CaMKII in dendritic spines
Penny, C. J., & Gold, M. G. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.05.010 · Cited by 34
Synaptic GluN2B/CaMKII-α Signaling Induces Synapto-Nuclear Transport of ERK and Jacob
da Rosa, M. M., Yuanxiang, P., Brambilla, R., Kreutz, M. R., & Karpova, A. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00066 · Cited by 34
Seward, M. E., Easley, C. A., McLeod, J. J. A., Myers, A. L., & Tombes, R. M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.06.037 · Cited by 32
Casanova, J. R., Nishimura, M., & Swann, J. W. (2013) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2013.10.004 · Cited by 34
Cai, Q., Chen, X., Zhu, S., Nicoll, R. A., & Zhang, M. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112146 · Cited by 31
Changes in the Adult GluN2B Associated Proteome following Adolescent Intermittent Ethanol Exposure
Swartzwelder, H. S., Risher, M.-L., Miller, K. M., Colbran, R. J., Winder, D. G., & Wills, T. A. (2016) · PLOS ONE · doi:10.1371/journal.pone.0155951 · Cited by 31
Interactions between calmodulin and neurogranin govern the dynamics of CaMKII as a leaky integrator
Ordyan, M., Bartol, T., Kennedy, M. B., Rangamani, P., & B, T. J. S. A. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1008015 · Cited by 28
Moro, A., van Woerden, G. M., Toonen, R. F. G., & Verhage, M. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000826 · Cited by 32
Kinase Signaling in Dendritic Development and Disease
Nourbakhsh, K., & Yadav, S. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.624648 · Cited by 31
β-adrenergic signaling broadly contributes to LTP induction
Jędrzejewska‐Szmek, J., Luczak, V., Abel, T. G., & Blackwell, K. T. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005657 · Cited by 30
Architectural Dynamics of CaMKII-Actin Networks
Khan, S., Downing, K. H., & Molloy, J. E. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.11.006 · Cited by 29
Characterization of CaMKIIα holoenzyme stability
Torres‐Ocampo, A. P., Özden, C., Hommer, A., Gardella, A. E., Lapinskas, E., Samkutty, A., Esposito, E. A., Garman, S. C., & Stratton, M. M. (2020) · Protein Science · doi:10.1002/pro.3869 · Cited by 30
Jinglong, T., Weijuan, G., Li, J., Tao, Q., Hongbo, Z., & Liu, S. (2013) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2013.09.002 · Cited by 30
CaMK-II oligomerization potential determined using CFP/YFP FRET
Lantsman, K., & Tombes, R. M. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.08.005 · Cited by 30
Cho, M., Cao, X., Wang, D., & Tsien, J. Z. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703344104 · Cited by 30
Zheng, Q., Zhang, H., Zhao, H., Chen, Y., Yang, H., Li, T., Cai, Q., Chen, Y., Wang, Y., Zhang, M., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.12.005 · Cited by 32
Sequestration of CaMKII in dendritic spines in silico
Khan, S., Zou, Y., Amjad, A., Gardezi, A., Smith, C. L., Winters, C., & Reese, T. S. (2011) · Journal of Computational Neuroscience · doi:10.1007/s10827-011-0323-2 · Cited by 29
Role 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
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Mora, R. J., Roberts, R. W., & Arnold, D. B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2108-13.2013 · Cited by 28
In and out of the postsynaptic region: signalling proteins on the move
Meyer, T., & Shen, K. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01764-5 · Cited by 28
Self-citationSignaling to the microtubule cytoskeleton: An unconventional role for C a MKII
McVicker, D. P., Millette, M. M., & Dent, E. W. (2014) · Developmental Neurobiology · doi:10.1002/dneu.22227 · Cited by 27
Nicole, O., Bell, D. M., Lesté-Lasserre, T., Doat, H., Guillemot, F., & Pacary, E. (2018) · Molecular Psychiatry · doi:10.1038/s41380-018-0046-0 · Cited by 28
Ischemia-elicited Oxidative Modulation of Ca2+/Calmodulin-dependent Protein Kinase II
Shetty, P. K., Huang, F. L., & Huang, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708479200 · Cited by 27
Lichtman, J. W., & Smith, S. J. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.040 · Cited by 26
Wang, P., Wu, Y., Zhou, T.-H., Sun, Y., & Pei, G. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01634-3 · Cited by 27
Downregulation of δ CaM kinase II in human tumor cells
Tombes, R. M., Mikkelsen, R. B., Jarvis, W. D., & Grant, S. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(99)00113-5 · Cited by 27
Imaging plasma membrane proteins in large membrane patches of Xenopus oocytes
Singer‐Lahat, D., Dascal, N., Mittelman, L. A., Peleg, S., & Lotan, I. (2000) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s004240000341 · Cited by 26
Zemoura, K., Balakrishnan, K. R., Grampp, T., & Benke, D. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1142-5 · Cited by 26
Guptaroy, B., Marwaha, N., Pla, M., Wang, Z., Nelson, H. B., Beckingham, K., & Griffith, L. C. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00115-7 · Cited by 26
A diffusion-activation model of CaMKII translocation waves in dendrites
Earnshaw, B. A., & Bressloff, P. C. (2009) · Journal of Computational Neuroscience · doi:10.1007/s10827-009-0188-9 · Cited by 25
Shioda, N., Sawai, M., Ishizuka, Y., Shirao, T., & Fukunaga, K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664920 · Cited by 25
Amphetamine sensitization elevates CaMKIIß mRNA
Greenstein, R., Novak, G., & Seeman, P. M. (2007) · Synapse · doi:10.1002/syn.20429 · Cited by 25
Metadata
- Authors
- Shen, K., Teruel, M. N., Subramanian, K., & Meyer, T.
- Affiliations
- Duke Medical Center (US)
- Corresponding author
- Meyer, Tobias
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1998-09
- Volume
- 21
- Issue
- 3
- Pages
- 593-606
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2146831587
- Cited by
- 350
- References
- 61
- Citations by year
- 2026: 7 · 2025: 4 · 2024: 5 · 2023: 9 · 2022: 9 · 2021: 6 · 2020: 20 · 2019: 14 · 2018: 18 · 2017: 10 · 2016: 7 · 2015: 12 · 2014: 9 · 2013: 21 · 2012: 14
- FWCI
- 5.41
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (2r01gm051457-04)
- National Institute of General Medical Sciences (GM-48113, GM 51457)
- 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 › Molecular Biology › Signaling Pathways in Disease
- Keywords
- CaMKIIβ, CaMKIIα, CaMKII isoforms, hetero-oligomers, F-actin binding, dendritic spines, actin cytoskeleton, protein localization, synaptic plasticity, long-term potentiation, neuroplasticity
- MeSH terms
- Actins, Animals, Cloning, Molecular, Cytoskeleton, Dendrites, Isoenzymes, Luminescent Proteins, Nerve Fibers, Neurons, Phosphorylation, Recombinant Fusion Proteins, Synapses, Transcription, Genetic, Protein Biosynthesis, Tumor Cells, Cultured, 3T3 Cells, Calcium-Calmodulin-Dependent Protein Kinases, Macromolecular Substances, Green Fluorescent Proteins, Mice, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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