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Structure of the CaMKIIδ/Calmodulin Complex Reveals the Molecular Mechanism of CaMKII Kinase Activation
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UNLABELLED: Long-term potentiation (LTP), a long-lasting enhancement in communication between neurons, is considered to be the major cellular mechanism underlying learning and memory. LTP triggers high-frequency calcium pulses that result in the activation of Calcium/Calmodulin (CaM)-dependent kinase II (CaMKII). CaMKII acts as a molecular switch because it remains active for a long time after the return to basal calcium levels, which is a unique property required for CaMKII function. Here we describe the crystal structure of the human CaMKIIdelta/Ca2+/CaM complex, structures of all four human CaMKII catalytic domains in their autoinhibited states, as well as structures of human CaMKII oligomerization domains in their tetradecameric and physiological dodecameric states. All four autoinhibited human CaMKIIs were monomeric in the determined crystal structures but associated weakly in solution. In the CaMKIIdelta/Ca2+/CaM complex, the inhibitory region adopted an extended conformation and interacted with an adjacent catalytic domain positioning T287 into the active site of the interacting protomer. Comparisons with autoinhibited CaMKII structures showed that binding of calmodulin leads to the rearrangement of residues in the active site to a conformation suitable for ATP binding and to the closure of the binding groove for the autoinhibitory helix by helix alphaD. The structural data, together with biophysical interaction studies, reveals the mechanism of CaMKII activation by calmodulin and explains many of the unique regulatory properties of these two essential signaling molecules. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3-D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the Web plugin are available in Text S1.
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“As is the case with many kinases, CaMKII contains an autoinhibitory regulatory segment (FIGURE 2, A, B1, AND B2) that binds across the substrate binding groove, whose structure and function have been delineated by peptides, mutations, and crystallography (71–77).”
From Synaptic memory and CaMKII (2023) · cites this paper as [75]
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2 retracted
Wang, C., Li, N., Liu, X., Zheng, Y., & Cao, X. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800436200 · Cited by 68
RetractedMa, S., Yang, Y., Wang, C., Ning, H., Gu, L., Zhong, H., Cai, Z., Wang, Q., Zhang, Q., Li, N., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028621 · Cited by 35
RetractedRefinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145
Likelihood-enhanced fast translation functions
McCoy, A. J., Grosse‐Kunstleve, R. W., Storoni, L. C., & Read, R. J. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905001617 · Cited by 1,641
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
Active and Inactive Protein Kinases: Structural Basis for Regulation
Johnson, L. N., Noble, M. E. M., & Owen, D. J. (1996) · Cell · doi:10.1016/s0092-8674(00)81092-2 · Cited by 1,396
Inhibition of Postsynaptic PKC or CaMKII Blocks Induction But Not Expression of LTP
Malinow, R., Schulman, H., & Tsien, R. W. (1989) · Science · doi:10.1126/science.2549638 · Cited by 1,325
A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.048 · Cited by 1,122
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
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Kastritis, P. L., Rodrigues, J., Folkers, G. E., Boelens, R., & Bonvin, A. M. J. J. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.04.017 · Cited by 145
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Stratton, M., Lee, I.-H., Bhattacharyya, M., Christensen, S. M., Chao, L. H., Schulman, H., Groves, J. T., & Kuriyan, J. (2014) · eLife · doi:10.7554/elife.01610 · Cited by 114
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Eberhardt, R. Y., Chang, Y., Bateman, A. G., Murzin, A. G., Axelrod, H. L., Hwang, W. C., & Aravind, L. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-327 · Cited by 69
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Ross, F. A., Hawley, S. A., Auciello, F. R., Gowans, G. J., Atrih, A., Lamont, D. J., & Hardie, D. G. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.05.021 · Cited by 71
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Marshall, C. B., Nishikawa, T., Osawa, M., Stathopulos, P. B., & Ikura, M. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.106 · Cited by 64
Sałaciak, K., Koszałka, A., Żmudzka, E., & Pytka, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094307 · Cited by 67
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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
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Özden, C., Sloutsky, R., Mitsugi, T., Santos, N., Agnello, E., Gaubitz, C., Foster, J., Lapinskas, E., Esposito, E. A., Saneyoshi, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111064 · Cited by 61
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Ingram, J. R., Knockenhauer, K. E., Markus, B. M., Mandelbaum, J., Ramek, A., Shan, Y., Shaw, D. E., Schwartz, T., Ploegh, H. L., & Lourido, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1505914112 · Cited by 60
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Piljić, A., de Diego, I., Wilmanns, M., & Schultz, C. (2011) · ACS Chemical Biology · doi:10.1021/cb100402n · Cited by 57
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Gógl, G., Alexa, A., Kiss, B., Katona, G., Kovács, M., Bodor, A., Reményi, A., & Nyitray, L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.684928 · Cited by 53
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Hoffman, L., Stein, R. A., Colbran, R. J., & Mchaourab, H. S. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.40 · Cited by 54
Chang, A. N., Mahajan, P., Knapp, S., Barton, H., Sweeney, H. L., Kamm, K. E., & Stull, J. T. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600633113 · Cited by 54
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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
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
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Wang, W., Li, J., Sun, Q., Yu, X., Zhang, W., Jia, N., An, C., Li, Y., Dong, Y., Han, F., et al. (2017) · Nature Plants · doi:10.1038/nplants.2017.11 · Cited by 45
Pigott, C. R., Mikolajek, H., Moore, C. E., Finn, S. J., Phippen, C. W., Werner, J. M., & Proud, C. G. (2012) · Biochemical Journal · doi:10.1042/bj20111536 · Cited by 48
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Temmerman, K., Simon, B., & Wilmanns, M. (2013) · FEBS Journal · doi:10.1111/febs.12384 · Cited by 44
Xu, Q., Malecka, K. L., Fink, L. S., Jordan, E. J., Duffy, E. M., Kolander, S., Peterson, J. R., & Dunbrack, R. L. (2015) · Science Signaling · doi:10.1126/scisignal.aaa6711 · Cited by 43
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Colcombet, J., Sözen, C., & Heribert Hirt, A. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.01941 · Cited by 42
Jiao, 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
The selenoprotein methionine sulfoxide reductase B1 (MSRB1)
Tarrago, L., Kaya, A., Kim, H.-Y., Manta, B., Lee, B.-C., & Gladyshev, V. N. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.08.043 · Cited by 39
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McCoy, F. P. G., Darbandi, R., Lee, H. C., Bharatham, K., Moldoveanu, T., Grace, C. R., Dodd, K., Lin, W., Chen, S.-I., Tangallapally, R. P., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.043 · Cited by 40
Proietti Onori, M., Koopal, B., Everman, D. B., Worthington, J. D., Jones, J. R., Ploeg, M. A., Mientjes, E., van Bon, B. W., Kleefstra, T., Schulman, H., et al. (2018) · Human Mutation · doi:10.1002/humu.23647 · Cited by 39
Feng, W., Liu, Y., Ding, Y., Mao, G., Zhao, T., Chen, K., Qiu, X., Xu, T., Zhao, X., Wu, X., et al. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02683-9 · Cited by 39
RIP1/RIP3/MLKL-mediated necroptosis contributes to vinblastine-induced myocardial damage
Zhou, H., Liu, L., Ma, X., Wang, J., Yang, J., Zhou, X., Yang, Y., & Liu, H. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03985-3 · Cited by 42
Ca2+ signaling in the myocardium by (redox) regulation of PKA/CaMKII
Johnston, A. S., Lehnart, S. E., & Burgoyne, J. R. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00166 · Cited by 39
Structural assembly of the signaling competent ERK2–RSK1 heterodimeric protein kinase complex
Alexa, A., Gógl, G., Glatz, G., Garai, Á., Zeke, A., Varga, J. M., Dudás, E. F., Jeszenői, N., Bodor, A., Hetényi, C., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417571112 · Cited by 42
Ma, C., Tang, K., Liu, Q., Zhu, R., & Cao, Z. (2013) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12124 · Cited by 38
CaMKII regulation of cardiac K channels
Mustroph, J., Maier, L. S., & Wagner, S. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00020 · Cited by 37
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Rigter, P. M. F., de Konink, C., Dunn, M. J., Onori, M. P., Humberson, J. B., Thomas, M., Barnes, C., Prada, C. E., Weaver, K. N., Ryan, T. D., et al. (2024) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2023.12.016 · Cited by 36
Zhu, L. J., Klutho, P. J., Scott, J. A., Xie, L., Luczak, E. D., Dibbern, M. E., Prasad, A. M., Jaffer, O. A., Venema, A. N., Nguyen, E. K., et al. (2014) · Vascular Pharmacology · doi:10.1016/j.vph.2014.01.001 · Cited by 36
Chen, L., Liang, W., Chen, S., Li, R., Tan, J.-L., Xu, P., Luo, L.-F., Wang, L., Yu, S., Meng, G., et al. (2014) · Nature Communications · doi:10.1038/ncomms4811 · Cited by 38
Wang, X., Marks, C. R., Perfitt, T. L., Nakagawa, T., Lee, A., Jacobson, D. A., & Colbran, R. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.788331 · Cited by 36
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Self-citationStructural Characterization of the Interaction of Human Lactoferrin with Calmodulin
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Metadata
- Authors
- Rellos, P., Pike, A. C. W., Niesen, F. H., Salah, E., Lee, W. H., von Delft, F., & Knapp, S.
- Affiliations
- University of Oxford (GB)
- Corresponding author
- Knapp, Stefan
- Venue
- PLoS Biology
- Publisher
- Public Library of Science (PLoS)
- Published
- 2010-07-27
- Volume
- 8
- Issue
- 7
- Pages
- e1000426
- ISSN
- 1544-9173 (ISSN-L)
- 1545-7885
- PMC
- PMC2910593
- OpenAlex
- W1989492234
- Cited by
- 279
- References
- 62
- Citations by year
- 2026: 10 · 2025: 23 · 2024: 14 · 2023: 21 · 2022: 14 · 2021: 32 · 2020: 19 · 2019: 14 · 2018: 15 · 2017: 19 · 2016: 11 · 2015: 12 · 2014: 22 · 2013: 20 · 2012: 16
- FWCI
- 6.78
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Oxford University Research Archive (ORA) (University of Oxford) (submittedVersion)
- Funders
- GlaxoSmithKline
- Ontario Innovation Trust
- Genome Canada (1097737)
- Wellcome Trust (1097737)
- Ontario Genomics
- Ontario Genomics Institute
- Stiftelsen för Strategisk Forskning
- Karolinska Institutet
- Knut och Alice Wallenbergs Stiftelse
- Paul Scherrer Institut
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- CaMKII, CaMKIIδ, calmodulin, kinase activation, autoinhibition, long-term potentiation, calcium signaling, protein complex structure, catalytic domain, oligomerization domain, ATP binding, learning and memory
- MeSH terms
- Calcium, Calmodulin, Calorimetry, Enzyme Activation, Humans, Isoenzymes, Models, Molecular, Phosphorylation, Phosphothreonine, Protein Binding, Substrate Specificity, Protein Structure, Secondary, Catalytic Domain, Protein Structure, Quaternary, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Protein Multimerization
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