DAPK1 Mediates LTD by Making CaMKII/GluN2B Binding LTP Specific
Open accessAbstract
The death-associated protein kinase 1 (DAPK1) is a potent mediator of neuronal cell death. Here, we find that DAPK1 also functions in synaptic plasticity by regulating the Ca 2+ /calmodulin (CaM)-dependent protein kinase II (CaMKII). CaMKII and T286 autophosphorylation are required for both long-term potentiation (LTP) and depression (LTD), two opposing forms of synaptic plasticity underlying learning, memory, and cognition. T286-autophosphorylation induces CaMKII binding to the NMDA receptor (NMDAR) subunit GluN2B, which mediates CaMKII synaptic accumulation during LTP. We find that the LTP specificity of CaMKII synaptic accumulation is due to its LTD-specific suppression by calcineurin (CaN)-dependent DAPK1 activation, which in turn blocks CaMKII binding to GluN2B. This suppression is enabled by competitive DAPK1 versus CaMKII binding to GluN2B. Negative regulation of DAPK1/GluN2B binding by Ca 2+ /CaM results in synaptic DAPK1 removal during LTP but retention during LTD. A pharmacogenetic approach showed that suppression of CaMKII/GluN2B binding is a DAPK1 function required for LTD.
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DAPK1 plays a role in LTD, where its activation via calcineurin-dependent dephosphorylation leads to GluN2B phosphorylation at Ser-1303, strengthening DAPK1 interaction and preventing CaMKII binding.
“DAPK1 also plays a role in LTD, where its activation via calcineurin-dependent dephosphorylation leads to GluN2B phosphorylation at Ser-1303, strengthening DAPK1 interaction and preventing CaMKII binding.”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [54]
DAPK1 functions as a refined physiological regulator during LTD, where its recruitment to GluN2B prevents CaMKII accumulation in the spine, thereby enabling bidirectional control of synaptic strength.
“Beyond its pathological role in excitotoxicity, DAPK1 functions as a refined physiological regulator during long-term depression (LTD), where its recruitment to GluN2B prevents CaMKII accumulation in the spine, thereby enabling bidirectional control of synaptic strength [48,54].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [54]
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Malenka, R. C., & Bear, M. F. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.012 · Cited by 3,968 · see citing works
Synaptic Plasticity and Memory: An Evaluation of the Hypothesis
Martin, S. J., Grimwood, P. D., & Morris, R. G. M. (2000) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.23.1.649 · Cited by 2,794 · see citing works
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 · see citing works
The Molecular and Systems Biology of Memory
Kandel, E. R., Dudai, Y., & Mayford, M. R. (2014) · Cell · doi:10.1016/j.cell.2014.03.001 · Cited by 1,134 · see citing works
Involvement of a calcineurin/ inhibitor-1 phosphatase cascade in hippocampal long-term depression
Mulkey, R. M., Endo, S., Shenolikar, S., & Malenka, R. C. (1994) · Nature · doi:10.1038/369486a0 · Cited by 1,083 · see citing works
Autophosphorylation at Thr <sup>286</sup> 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 · 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
Long-term depression in the CNS
Collingridge, G. L., Peineau, S., Howland, J. G., & Wang, Y. T. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2867 · Cited by 926 · see citing works
Derkach, 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
The Cognitive Neuroscience of Human Memory Since H.M.
Squire, L. R., & Wixted, J. T. (2011) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-061010-113720 · Cited by 749 · 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
Self-citationLTP Inhibits LTD in the Hippocampus via Regulation of GSK3β
Peineau, S., Taghibiglou, C., Bradley, C. A., Wong, T. P., Liu, L., Lu, J., Lo, E., Wu, D., Saule, E., Bouschet, T., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.029 · Cited by 690 · 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
Shen, K., & Meyer, T. (1999) · Science · doi:10.1126/science.284.5411.162 · Cited by 673 · see citing works
Lee, H.-K., Kameyama, K., Huganir, R. L., & Bear, M. F. (1998) · Neuron · doi:10.1016/s0896-6273(00)80632-7 · Cited by 668 · see citing works
Li, Z., Jo, J., Jia, J., Lo, S., Whitcomb, D. J., Jiao, S., Cho, K., & Sheng, M. (2010) · Cell · doi:10.1016/j.cell.2010.03.053 · Cited by 533 · 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
Zeng, H., Chattarji, S., Barbarosie, M., Rondi-Reig, L., Philpot, B. D., Miyakawa, T., Bear, M. F., & Tonegawa, S. (2001) · Cell · doi:10.1016/s0092-8674(01)00585-2 · Cited by 498 · see citing works
DAPK1 Interaction with NMDA Receptor NR2B Subunits Mediates Brain Damage in Stroke
Tu, W., Xu, X., Peng, L., Zhong, X., Zhang, W., Soundarapandian, M. M., Belal, C., Wang, M., Jia, N., Zhang, W., et al. (2010) · Cell · doi:10.1016/j.cell.2009.12.055 · Cited by 493 · see citing works
Strack, S., & Colbran, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.33.20689 · Cited by 466 · see citing works
The role of calmodulin as a signal integrator for synaptic plasticity
Xia, Z., & Storm, D. R. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1647 · Cited by 441 · see citing works
The Death-Associated Protein Kinases: Structure, Function, and Beyond
Bialik, S., & Kimchi, A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142615 · Cited by 441 · see citing works
Malgaroli, A., & Tsien, R. (1992) · Nature · doi:10.1038/357134a0 · Cited by 385 · see citing works
Leonard, A. S., Lim, I. A., Hemsworth, D. E., Horne, M. C., & Hell, J. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3239 · Cited by 385 · see citing works
Self-citationRecombinant Probes for Visualizing Endogenous Synaptic Proteins in Living Neurons
Gross, G. G., Junge, J. A., Mora, R. J., Kwon, H., Olson, C. A., Takahashi, T. T., Liman, E. R., Ellis‐Davies, G. C. R., McGee, A. W., Sabatini, B. L., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.04.017 · Cited by 357 · see citing works
Strack, S., McNeill, R. B., & Colbran, R. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001471200 · 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 351 · see citing works
Self-citationCaMKII 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
Self-citationMechanism of Ca2+/calmodulin-dependent kinase II regulation of AMPA receptor gating
Kristensen, A. S., Jenkins, M. A., Banke, T. G., Schousboe, A., Makino, Y., Johnson, R. C., Huganir, R., & Traynelis, S. F. (2011) · Nature Neuroscience · doi:10.1038/nn.2804 · Cited by 286 · see citing works
Kameyama, K., Lee, H.-K., Bear, M. F., & Huganir, R. L. (1998) · Neuron · doi:10.1016/s0896-6273(00)80633-9 · Cited by 283 · see citing works
Gözüaçık, D., Bialik, S., Raveh, T. B., Mitou, G., Shohat-Ophir, G., Sabanay, H., Mizushima, N., Yoshimori, T., & Kimchi, A. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.121 · Cited by 259 · 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
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 253 · see citing works
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 · see citing works
Self-citationLocal Pruning of Dendrites and Spines by Caspase-3-Dependent and Proteasome-Limited Mechanisms
Ertürk, A., Wang, Y., & Sheng, M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3121-13.2014 · Cited by 231 · see citing works
Sanderson, J. L., Gorski, J. A., & Dell’Acqua, M. L. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.043 · Cited by 210 · see citing works
Coultrap, S. J., Freund, R. K., O’Leary, H., Sanderson, J. L., Roche, K. W., Dell’Acqua, M. L., & Bayer, K. U. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.01.005 · Cited by 207 · see citing works
Self-citationDual 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 · see citing works
Self-citationThe role of calcium–calmodulin kinase II in three forms of synaptic plasticity
Stevens, C. F., Tonegawa, S., & Wang, Y. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00153-6 · Cited by 183 · see citing works
Interactions between the NR2B Receptor and CaMKII Modulate Synaptic Plasticity and Spatial Learning
Zhou, Y., Takahashi, E., Li, W., Halt, A., Wiltgen, B., Ehninger, D., Li, G.-D., Hell, J. W., Kennedy, M. B., & Silva, A. J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4486-07.2007 · Cited by 179 · see citing works
Self-citationPoncer, J. C., Esteban, J. A., & Malinow, R. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-11-04406.2002 · Cited by 177 · see citing works
Shohat-Ophir, G., Spivak-Kroizman, T. R., Cohen, O., Bialik, S., Shani, G., Berissi, H., Eisenstein, M., & Kimchi, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105133200 · Cited by 153 · see citing works
Pelled, D., Raveh, T. B., Riebeling, C., Fridkin, M., Berissi, H., Futerman, A. H., & Kimchi, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m104677200 · Cited by 143 · see citing works
Selective translocation of Ca 2+ /calmodulin protein kinase IIα (CaMKIIα) to inhibitory synapses
Marsden, K. C., Shemesh, A., Bayer, K. U., & Carroll, R. C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010346107 · Cited by 135 · see citing works
Self-citationShonesy, 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
Death-associated Protein Kinase Is Activated by Dephosphorylation in Response to Cerebral Ischemia
Shamloo, M., Soriano, L., Wieloch, T. W., Nikolich, K., Urfer, R., & Oksenberg, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505804200 · Cited by 117 · see citing works
Molecular Basis of the Death-Associated Protein Kinase–Calcium/Calmodulin Regulator Complex
de Diego, I., Kuper, J., Bakalova, N., Kursula, P., & Wilmanns, M. (2010) · Science Signaling · doi:10.1126/scisignal.2000552 · Cited by 104 · see citing works
Kim, B. M., You, M.-H., Chen, C.-H., Lee, S., Hong, Y., Hong, Y., Kimchi, A., Zhou, X. Z., & Lee, T. H. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.216 · Cited by 98 · see citing works
Lü, W., Isozaki, K., Roche, K. W., & Nicoll, R. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016289107 · Cited by 92 · see citing works
Long-term potentiation in cultured hippocampal neurons
Molnár, E. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.07.017 · Cited by 85 · see citing works
Neuronal Activity and CaMKII Regulate Kinesin-Mediated Transport of Synaptic AMPARs
Hoerndli, F. J., Wang, R., Mellem, J. E., Kallarackal, A. J., Brockie, P. J., Thacker, C. M., Madsen, D. M., & Maricq, A. V. (2015) · Neuron · doi:10.1016/j.neuron.2015.03.011 · Cited by 84 · see citing works
Coultrap, S. J., & Bayer, K. U. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.558254 · Cited by 81 · see citing works
Self-citationMolecular Characterization of Calmodulin Trapping by Calcium/Calmodulin-dependent Protein Kinase II
Singla, S., Hudmon, A., Goldberg, J. M., Smith, J. L., & Schulman, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101744200 · Cited by 78 · see citing works
O’Leary, H., Liu, W. H., Rorabaugh, J. M., Coultrap, S. J., & Bayer, K. U. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.233668 · Cited by 76 · see citing works
Self-citationThe CaMKII/GluN2B Protein Interaction Maintains Synaptic Strength
Barcomb, K., Hell, J. W., Benke, T. A., & Bayer, K. U. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.734822 · Cited by 76 · see citing works
Self-citationAKAP150‐anchored PKA activity is important for LTD during its induction phase
Lü, Y., Zhang, M., Lim, I. A., Hall, D. D., Allen, M., Medvedeva, Y. V., McKnight, G. S., Usachev, Y. M., & Hell, J. W. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.151662 · Cited by 72 · see citing works
Self-citationBialik, S., & Kimchi, A. (2013) · APOPTOSIS · doi:10.1007/s10495-013-0926-3 · Cited by 67 · see citing works
Kim, B. M., You, M., Chen, C.-H., Suh, J., Tanzi, R. E., & Lee, T. H. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw114 · Cited by 52 · see citing works
Barcomb, K., Buard, I., Coultrap, S. J., Kulbe, J. R., O'Leary, H., Benke, T. A., & Bayer, K. U. (2014) · The FASEB Journal · doi:10.1096/fj.14-250407 · Cited by 52 · see citing works
Self-citationSchumacher, A. M., Velentza, A. V., Watterson, D. M., & Wainwright, M. S. (2002) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(02)00453-3 · Cited by 50 · see citing works
Recombinant Probes Reveal Dynamic Localization of CaMKIIα within Somata of Cortical Neurons
Mora, R. J., Roberts, R. W., & Arnold, D. B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2108-13.2013 · Cited by 28 · see citing works
Ca2+/Calmodulin-Dependent Protein Kinase II (CaMKII)
Coultrap, S. J., & Bayer, K. U. (2012) · Neuromethods · doi:10.1007/978-1-61779-824-5_4 · Cited by 22 · see citing works
Self-citationBarcomb, K., Coultrap, S. J., & Bayer, K. U. (2013) · Molecular Pharmacology · doi:10.1124/mol.113.089045 · Cited by 22 · see citing works
Self-citationCaMKII Binding to GluN2B Is Differentially Affected by Macromolecular Crowding Reagents
Goodell, D. J., Eliseeva, T. A., Coultrap, S. J., & Bayer, K. U. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096522 · Cited by 16 · see citing works
Self-citationBarcomb, K., Goodell, D. J., Arnold, D. B., & Bayer, K. U. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13263 · Cited by 14 · see citing works
Self-citationDevelopmental restoration of LTP deficits in heterozygous CaMKIIα KO mice
Goodell, D. J., Benke, T. A., & Bayer, K. U. (2016) · Journal of Neurophysiology · doi:10.1152/jn.00518.2016 · Cited by 12 · see citing works
Self-citation
Flagged first, then by citations
1 of the 67 references couldn’t be matched to a known paper.
Research works printed but not linked: 5
- Barcomb K Buard I Coultrap SJ Kulbe JR O’Leary H Benke TA Bayer KU 2014 Autonomous CaMKII requires further stimulation by Ca2+/calmodulin for enhancing synaptic strength The FASEB Journal 28 3810 3819 24843070 PMC4101658
- Malenka RC Bear MF 2004 LTP and LTD: an embarrassment of riches Neuron 44 5 21 15450156
- Marsden KC Shemesh A Bayer KU Carroll RC 2010 Selective translocation of Ca2+/calmodulin protein kinase IIalpha (CaMKIIalpha) to inhibitory synapses Proc. Natl. Acad. Sci. U.S.a 107 20559 20564 21059908 PMC2996683
- Shonesy BC Jalan-Sakrikar N Cavener VS Colbran RJ 2014 CaMKII: a molecular substrate for synaptic plasticity and memory Prog Mol Biol Transl Sci 122 61 87 24484698
- Squire LR Wixted JT 2011 The cognitive neuroscience of human memory since HM Annu. Rev. Neurosci 34 259 21456960 PMC3192650
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Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000131 · Cited by 686 · see citing works
CaMKII: a central molecular organizer of synaptic plasticity, learning and memory
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Self-citationCaM Kinase: Still Inspiring at 40
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Self-citationPlasticity of Spine Structure: Local Signaling, Translation and Cytoskeletal Reorganization
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Vieira, M., Yong, X. L. H., Roche, K. W., & Anggono, V. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14970 · Cited by 151 · see citing works
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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
Self-citationNicoll, R. A., & Schulman, H. (2023) · Physiological Reviews · doi:10.1152/physrev.00034.2022 · Cited by 126 · see citing works
“Another form consists of the competition of DAPK1 (death-associated protein kinase 1) with CaMKII for binding to GluN2B (400).”
BackgroundDeath‐associated protein kinase (DAPK) family modulators: Current and future therapeutic outcomes
Farag, A. K., & Roh, E. J. (2018) · Medicinal Research Reviews · doi:10.1002/med.21518 · Cited by 115 · see citing works
Zong, P., Feng, J., Yue, Z., Li, Y., Wu, G., Sun, B., He, Y., Miller, B. A., Yu, A. S., Su, Z., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.03.021 · Cited by 102 · see citing works
Mira, R. G., & Cerpa, W. F. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00924-0 · Cited by 96 · see citing works
Rostas, J. A. P., & Skelding, K. A. (2023) · Cells · doi:10.3390/cells12030401 · Cited by 85 · see citing works
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Sanderson, J. L., Freund, R. K., Gorski, J. A., & Dell’Acqua, M. L. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109786 · Cited by 60 · see citing works
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Xu, L.-Z., Li, B.-Q., & Jia, J.-P. (2019) · Molecular Neurobiology · doi:10.1007/s12035-018-1242-2 · Cited by 42 · see citing works
Mechanisms and Role of Dendritic Membrane Trafficking for Long-Term Potentiation
Hiester, B. G., Becker, M. I., Bowen, A. B., Schwartz, S. L., & Kennedy, M. J. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00391 · Cited by 37 · see citing works
GluN2B-containing NMDARs in the mammalian brain: pharmacology, physiology, and pathology
Ge, Y., & Wang, Y. T. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1190324 · Cited by 41 · see citing works
Long-Term Depression Is Independent of GluN2 Subunit Composition
Wong, J. M., & Gray, J. A. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0394-18.2018 · Cited by 39 · see citing works
CaMKII T286 phosphorylation has distinct essential functions in three forms of long-term plasticity
Cook, S. G., Rumian, N. L., & Bayer, K. U. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102299 · Cited by 31 · see citing works
Self-citationChowdhury, D., & Hell, J. W. (2019) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2019.00006 · Cited by 27 · see citing works
Self-citationRedox DAPK1 destabilizes Pellino1 to govern inflammation-coupling tubular damage during septic AKI
Hu, B., Wu, G., Shao, Z., Zheng, Y., Liu, J., Zhang, R., Hong, J., Yang, X., Sun, R.-H., & Mo, S. (2020) · Theranostics · doi:10.7150/thno.49870 · Cited by 27 · see citing works
Schmidt, M. E., Caron, N. S., Aly, A. E.-E., Lemarié, F. L., Cengio, L. D., Ko, Y., Lazic, N., Anderson, L. M., Nguyen, B., Raymond, L. A., et al. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.590569 · Cited by 25 · see citing works
Park, D. K., Petshow, S., Anisimova, M., Barragan, E. V., Gray, J. A., Stein, I. S., & Zito, K. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105772 · Cited by 23 · see citing works
Regulation of Synaptic NMDA Receptor Activity by Post-Translational Modifications
Tahiri, E., Corti, E., & Duarte, C. B. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04346-6 · Cited by 21 · see citing works
Zhang, L., Wang, Z., Song, C., Liu, H., Li, Y., Li, J., Yu, Y., Wang, G., & Cui, W. (2020) · Regional Anesthesia & Pain Medicine · doi:10.1136/rapm-2020-101883 · Cited by 21 · see citing works
Characterization of six CaMKIIα variants found in patients with schizophrenia
Brown, C. N., Cook, S. G., Allen, H. F., Crosby, K. C., Singh, T., Coultrap, S. J., & Bayer, K. U. (2021) · iScience · doi:10.1016/j.isci.2021.103184 · Cited by 28 · see citing works
Self-citationLiu, S., Liu, C., Xiong, L., Xie, J., Huang, C., Pi, R., Huang, Z., & Li, L. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.525615 · Cited by 22 · see citing works
LTP expression mediated by autonomous activity of GluN2B-bound CaMKII
Rumian, N. L., Barker, C. M., Larsen, M. E., Tullis, J. E., Freund, R. K., Taslimi, A., Coultrap, S. J., Tucker, C. L., Dell’Acqua, M. L., & Bayer, K. U. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114866 · Cited by 20 · see citing works
Self-citationTrimmer, J. S. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.11.004 · Cited by 17 · see citing works
Regulation of the NMDA receptor by its cytoplasmic domains: (How) is the tail wagging the dog?
Ishchenko, Y., Carrizales, M. G., & Koleske, A. J. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108634 · Cited by 21 · see citing works
Xu, L., Li, B., Li, F., Li, Y., Qin, W., Zhao, Y., & Jia, J. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220747 · Cited by 19 · see citing works
Liu, Y., Guo, W., & Hong, S. (2023) · The FASEB Journal · doi:10.1096/fj.202300847rr · Cited by 19 · see citing works
Miozzo, F., Murru, L., Maiellano, G., di Iasio, I., Zippo, A. G., Avendano, A. Z., Metodieva, V. D., Riccardi, S., D’Aliberti, D., Spinelli, S., et al. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.0491-24.2024 · Cited by 18 · see citing works
Zhou, Z., Bai, J., Zhong, S., Zhang, R., Kang, K., Zhang, X., Xu, Y., Zhao, C., & Zhao, M. (2021) · The EPMA Journal · doi:10.1007/s13167-021-00261-2 · Cited by 17 · see citing works
Loss of MsrB1 perturbs spatial learning and long-term potentiation/long-term depression in mice
Shi, T., Yang, Y., Zhang, Z.-H., Zhang, L., Song, J., Ping, Y., Du, X., Song, G.-L., Liu, Q., & Li, N. (2019) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2019.107104 · Cited by 16 · see citing works
The CaMKII K42M and K42R mutations are equivalent in suppressing kinase activity and targeting
Tullis, J. E., Rumian, N. L., Brown, C. N., & Bayer, K. U. (2020) · PLoS ONE · doi:10.1371/journal.pone.0236478 · Cited by 13 · see citing works
Self-citationGluN2B S1303 phosphorylation by CaMKII or DAPK1: No indication for involvement in ischemia or LTP
Tullis, J. E., Buonarati, O. R., Coultrap, S. J., Bourke, A. M., Tiemeier, E. L., Kennedy, M. J., Herson, P. S., & Bayer, K. U. (2021) · iScience · doi:10.1016/j.isci.2021.103214 · Cited by 13 · see citing works
Self-citationLarsen, M. E., Buonarati, O. R., Qian, H., Hell, J. W., & Bayer, K. U. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104706 · Cited by 13 · see citing works
Self-citationTullis, J. E., & Bayer, K. U. (2023) · iScience · doi:10.1016/j.isci.2023.106723 · Cited by 12 · see citing works
Self-citationSun, Y., Hao, M., Wu, H., Zhang, C., Dong, W., Li, S., Song, Z., & Tao, Y. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01236-2 · Cited by 12 · see citing works
Li, R., Zhi, S., Lan, G., Chen, X., Zheng, X., Hu, L., Wang, L., Zhang, T., Lee, T. H., Rao, S., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076542 · Cited by 11 · see citing works
Mei, Y., She, F., Zhang, L., Kim, G., Li, R., Zheng, X., Wang, Z., Chen, R., Wang, L., Chen, D., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07474-7 · Cited by 10 · see citing works
Brown, C. N., Rumian, N. L., Tullis, J. E., Coultrap, S. J., & Bayer, K. U. (2022) · iScience · doi:10.1016/j.isci.2022.104368 · Cited by 8 · see citing works
Self-citationZhou, S., Cui, X., Chen, J., Luo, M., Ouyang, W., Tong, J., Xie, Z., & Le, Y. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.02.017 · Cited by 9 · see citing works
Rumian, N. L., Brown, C. N., Hendry‐Hofer, T. B., Rossetti, T., Orfila, J. E., Tullis, J. E., Dwoskin, L. P., Buonarati, O. R., Lisman, J. E., Quillinan, N., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104693 · Cited by 9 · see citing works
Self-citationKeith, R. E., Wild, G. A., Keith, M. J., Chen, D., Pack, S., & Dumas, T. C. (2024) · Synapse · doi:10.1002/syn.22292 · Cited by 8 · see citing works
Postsynaptic signaling at glutamatergic synapses as therapeutic targets.
Ge, Y., & Wang, Y.-T. (2022) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2022.102585 · Cited by 7 · see citing works
Liu, Z., Zhang, J., Miao, L., Kong, Q., Liu, X., & Yu, L. (2022) · Brain Sciences · doi:10.3390/brainsci12080985 · Cited by 8 · see citing works
Young DAPK1 knockout mice have altered presynaptic function
Goodell, D. J., Tullis, J. E., & Bayer, K. U. (2021) · Journal of Neurophysiology · doi:10.1152/jn.00055.2021 · Cited by 7 · see citing works
Self-citationDendritic spine membrane proteome and its alterations in autistic spectrum disorder
Vallés, A. S., & Barrantes, F. J. (2022) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2021.09.003 · Cited by 7 · see citing works
Molecular Physiology of the Neuronal Synapse
Ramírez-Expósito, M. J., Cueto-Ureña, C., & Martínez-Martos, J. M. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48010088 · Cited by 6 · see citing works
“Beyond its pathological role in excitotoxicity, DAPK1 functions as a refined physiological regulator during long-term depression (LTD), where its recruitment to GluN2B prevents CaMKII accumulation in the spine, thereby enabling bidirectional control of synaptic strength [48,54].”
Tian, X., Wang, X., Chen, S., Sun, X., Shao, D., Zhang, K., Gao, Q., & Hao, L. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102886 · Cited by 6 · see citing works
CaMKII mechanisms that promote pathological LTP impairments
Larsen, M. E., Rumian, N. L., Quillinan, N., & Bayer, K. U. (2025) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2024.102961 · Cited by 6 · see citing works
Self-citationIs autism a PIN1 deficiency syndrome? A proposed etiological role for glyphosate
Seneff, S., Kyriakopoulos, A. M., & Nigh, G. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16140 · Cited by 6 · see citing works
Urrieta, E., & Escobar, M. L. (2021) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2021.107449 · Cited by 6 · see citing works
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 · see citing works
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 · see citing works
Tian, Y., Zheng, X., Li, R., Li, H., Shui, X., Wang, L., Chen, D., Lee, T. H., & Zhang, T. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03674-4 · Cited by 4 · see citing works
Zhang, X., Cai, W., Wang, C., & Tian, J. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108888 · Cited by 5 · see citing works
Positive Modulation of SK Channel Impedes Neuron-Specific Cytoskeletal Organization and Maturation
Shrestha, A., Sultana, R., Adeniyi, P. A., Lee, C. C., & Ogundele, O. M. (2020) · Developmental Neuroscience · doi:10.1159/000507989 · Cited by 3 · see citing works
Gupta, R. V., Begum, M. Y., Kumar, R., Gupta, J., Nagraik, R., Panda, S. P., Abomughaid, M. M., Lakhanpal, S., Avinash, D., Osmani, R. A. M., et al. (2025) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-025-10258-7 · Cited by 4 · see citing works
Aβ impairs the LTP-related movement of endogenous CaMKII but not of exogenous GFP-CaMKII
Brown, C. N., Chao, F.-Y., Quang, D., Rumian, N. L., Kleinjan, M. S., Coultrap, S. J., & Bayer, K. U. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-10-0443 · Cited by 2 · see citing works
Self-citationMolecular Mechanisms of Non-ionotropic NMDA Receptor SignalingPreprint
Stein, I. S., Park, D. K., Jahncke, J. N., Flores, J. C., & Zito, K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.08.898080 · Cited by 2 · see citing works
Brown, C. N., Blaine, R. E., Barker, C. M., Coultrap, S. J., & Bayer, K. U. (2025) · Molecular Pharmacology · doi:10.1016/j.molpha.2025.100029 · Cited by 1 · see citing works
Self-citationPacheco-Sánchez, B., Verheul-Campos, J., Vargas, A., Tovar, R., Rodríguez-Pozo, M., Navarro, J. A., López-Gambero, A. J., Baixerás, E., Serrano-Castro, P. J., Suárez, J., et al. (2025) · Nutrients · doi:10.3390/nu17183024 · Cited by 1 · see citing works
Shukla, S., & Singh, R. K. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-11933-5 · Cited by 1 · see citing works
CaMKII monomers are sufficient for GluN2B binding, co-condensation, and synaptic potentiation
Brown, C. N., Barker, C. M., Miller, C. N., Chao, F.-Y., Aoto, J. N., Coultrap, S. J., & Bayer, K. U. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.08.029 · Cited by 2 · see citing works
Self-citationKe, X., Ma, S., Zhang, Y., Yao, Y., Yu, H., Yu, D., & Pei, L. (2018) · Exploratory Research and Hypothesis in Medicine · doi:10.14218/erhm.2018.00018 · Cited by 1 · see citing works
Oxygen/glucose-deprivation causes long-term impairment of synaptic CaMKII movementPreprint
Buonarati, O. R., Quillinan, N., & Bayer, K. U. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.01.640973 · Cited by 1 · see citing works
Self-citationEssential regulatory functions of CaMKII T286 phosphorylation in LTP and two distinct forms of LTDPreprint
Cook, S. G., Rumian, N. L., & Bayer, K. U. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.03.474759
Self-citationCaMKII binding to GluN2B flips a β-adrenergic switch from synaptic depression to potentiationPreprint
Buonarati, O. R., Larsen, M. E., Qian, H., Hell, J. W., & Bayer, K. U. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.23.497296
Self-citationRumian, N. L., Brown, C. N., Hendry‐Hofer, T. B., Rossetti, T., Orfila, J. E., Tullis, J. E., Dwoskin, L. P., Buonarati, O. R., Lisman, J. E., Quillinan, N., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.23.523316
Self-citationCaMKII mechanisms in plasticity, learning and memory: Approaches and concepts
Bayer, K. U., Brown, C. N., & Giese, K.-P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15754-7.00057-2
Self-citationImpact of open channel blockers on the surface dynamics and organization of NMDA receptors
Fernandes, A. (2020) · theses.fr (ABES) · doi:10.70675/d12c14b2z7a80z4668z9c48z8e2c0e41c009 · Cited by 1 · see citing works
Interaction between synaptic and structural plasticity
Camus, C. (2021) · theses.fr (ABES) · doi:10.70675/6340fbbaz26d9z40d5zade8z917b9d9fd531
Synaptic Plasticity as a Function of the Temporal DerivativePreprint
Jang, J., Flores, J. C., Zito, K., & O’Reilly, R. C. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.05.730489
Death-associated protein kinase 1 in neurodegenerative disorders
Pandey, S. K., Singh, S., Shukla, S., & Singh, R. K. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44173-8.00017-6
Regulation of different kinases for Alzheimer's disease therapy: progresses and perspectives
Han, M., Liao, Q., He, S., Guo, L., Lu, Z., Wang, X., Sun, W., Duan, Y. B., Lyu, W., & Li, Q. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.110300
Peng, L., Li, Q., Li, Z., Bai, G., Tian, Y., & Zhou, S. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c11943
Sun, J., Gao, G., Wang, S., Li, S., Tang, J., Liu, H., & Tang, T.-S. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02776-4
- Authors
- Goodell, D. J., Zaegel, V., Coultrap, S. J., Hell, J. W., & Bayer, K. U.
- Affiliations
- University of Colorado Anschutz (US)
- University of California, Davis (US)
- Corresponding author
- Bayer, K. Ulrich
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 19
- Issue
- 11
- Pages
- 2231-2243
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC5549467
- OpenAlex
- W2625709293
- Cited by
- 88
- References
- 67
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 9 · 2023: 11 · 2022: 12 · 2021: 13 · 2020: 11 · 2019: 4 · 2018: 7 · 2017: 1
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship (California Digital Library) (submittedVersion, cc-by-nc-nd)
- Funders
- NIH (F31NS092265, R01MH097887, R01AG055357, R01NS081248, R01NS080851)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Health Sciences › Medicine › Pharmacology › Treatment of Major Depression
- Keywords
- DAPK1, CaMKII, GluN2B, NMDA receptor, long-term depression, long-term potentiation, synaptic plasticity, CaMKII autophosphorylation, calcineurin, Ca2+/calmodulin signaling, protein-protein binding
- MeSH terms
- Amino Acid Sequence, Animals, Humans, Memory, Neuronal Plasticity, Phosphorylation, Transfection, Receptors, N-Methyl-D-Aspartate, Long-Term Potentiation, Long-Term Synaptic Depression, Mice, Calcium-Calmodulin-Dependent Protein Kinase Type 2, HEK293 Cells, Death-Associated Protein Kinases
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