Functional Implications of the Subunit Composition of Neuronal CaM Kinase II
Open accessAbstract
The assembly of 6-12 subunits of Ca(2+)/calmodulin-dependent kinase II (CaM kinase II) into holoenzymes is an important structural feature of the enzyme and its postulated role as a molecular detector of Ca(2+) oscillations. Using single cell reverse transcriptase-polymerase chain reaction, we show that alpha- and beta-CaM kinase II mRNAs are simultaneously present in the majority of hippocampal neurons examined and that co-assembly of their protein products into heteromers is therefore possible. The subunit composition of CaM kinase II holoenzymes was analyzed by immunoprecipitation with subunit-specific monoclonal antibodies. Rat forebrain CaM kinase II consists of heteromers composed of alpha and beta subunits at a ratio of 2:1 and homomers composed of only alpha subunits. We examined the functional effect of the heteromeric assembly by analyzing the calmodulin dependence of autophosphorylation. Recombinant homomers of alpha- or beta-CaM kinase II, as well as of alternatively spliced beta isoforms, have distinct calmodulin dependences for autophosphorylation based on differences in their calmodulin affinities. Half-maximal autophosphorylation of alpha is achieved at 130 nM calmodulin, while that for beta occurs at 15 nM calmodulin. In CaM kinase II isolated from rat forebrain, however, the calmodulin dependence for autophosphorylation of the beta subunits is shifted toward that of alpha homomers. This suggests that Thr(287) in beta subunits is phosphorylated by alpha subunits present in the same holoenzyme. Once autophosphorylated, beta-CaM kinase II traps calmodulin by reducing the rate of calmodulin dissociation.
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In the forebrain the ratio is roughly 3 α to 1 β, and holoenzymes are composed of both subunits.
“In the forebrain the ratio is roughly 3 α to 1 β, and holoenyzmes are composed of both subunits (155–157).”
From Synaptic memory and CaMKII (2023) · cites this paper as [156]
The subunit-composition results report a 3:1 α:β ratio in material precipitated with the α-specific antibody and show that forebrain holoenzymes containing both subunits exist. The Discussion also says the preparation contains α-only homomers, so the claim is too broad if it means all holoenzymes contain both subunits; the paper reports a 2:1 ratio for the heteromers. (LLM, conf=0.86)
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BackgroundInfluentialAlternative splicing modulates the frequency‐dependent response of CaMKII to Ca2+ oscillations
Bayer, K. U., Koninck, P. D., & Schulman, H. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf360 · Cited by 112 · see citing works
Self-citationEshete, F., & Fields, R. D. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-17-06694.2001 · Cited by 97 · see citing works
“These isoforms differ in the variable domain of the protein (Brocke et al., 1999).”
BackgroundCaMKIIβ 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
“CaMKII subunits primarily coassemble with CaMKII to form hetero-oligomers (23).”
BackgroundLTP and adaptation to inactivity: Overlapping mechanisms and implications for metaplasticity
Thiagarajan, T. C., Lindskog, M., Malgaroli, A., & Tsien, R. W. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2006.07.030 · Cited by 99 · see citing works
Structural rearrangement of CaMKIIα catalytic domains encodes activation
Thaler, C., Koushik, S. V., Puhl, H. L., Blank, P. S., & Vogel, S. S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901913106 · Cited by 86 · see citing works
“Because CaMKII holoenzymes are thought to be composed of a mixture of - and -subunits (15, 31), the existence of catalytic domain pairing raises interesting possibilities regarding their function.”
BackgroundHouse, S., Ginnan, R., Armstrong, S. E., & Singer, H. (2007) · American Journal of Physiology - Cell Physiology · doi:10.1152/ajpcell.00606.2006 · Cited by 82
“Because CaMKII is expressed as large homo- and heteromultimeric holoenzymes, the subunit composition may confer subcellular targeting and specific protein interactions directing enzymatic activity to specific cellular compartments and functions (4, 6, 43).”
BackgroundCaMKII, 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 · see citing works
Nakayama, K., Kiyosue, K., & Taguchi, T. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4115-04.2005 · Cited by 84 · see citing works
“isoform of CaMKII ( CaMKII) has higher calmodulin sensitivity than isoform (Brocke et al., 1999), and reduction of neuronal activity can upregulate the expression of CaMKII within a few days in hippocampal neurons (Thiagarajan et al.”
BackgroundHoffman, L., Farley, M. M., & Waxham, M. N. (2013) · Biochemistry · doi:10.1021/bi3016586 · Cited by 76 · see citing works
Rostas, J. A. P., & Skelding, K. A. (2023) · Cells · doi:10.3390/cells12030401 · Cited by 85 · see citing works
“This can further fine tune CaMKII, as different CaMKII isoforms have different affinities for calmodulin [40], and also exhibit dif ering enzyme kinetics [43].”
BackgroundCAMK2-Dependent Signaling in Neurons Is Essential for Survival
Kool, M. J., Onori, M. P., Borgesius, N. Z., van de Bree, J. E., Elgersma, M., Nio, E., Bezstarosti, K., Buitendijk, G. H. S., Jolfaei, M. A., Demmers, J., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1341-18.2019 · Cited by 77 · see citing works
“With the difference in binding affinity for Calmodulin, which is 8-fold higher for CAMK2B homomers than for CAMK2A homomers (half-maximum autophosphorylation of CAMK2 is achieved at 15 vs 130 nM calmodulin, respectively; Brocke et al., 1999), the subunit composition of the CAMK2 holoenzyme determines the sensitivity f…”
BackgroundSchulman, H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3606-04.2004 · Cited by 71 · see citing works
“…composed of - and -CaMKII subunits as well as homomultimers of only one isoforms type, and these differ in catalytic and regulatory function (Brocke et al., 1999) and in targeting The expression ratio of CaM kinase isoforms changes during development (Miller and Kennedy, 1985; Wu and Cline,…”
BackgroundInfluentialSelf-citationGroth, 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 · see citing works
“Up-regulation of βCaMKII, which is approximately eightfold more sensitive to Ca/CaM than αCaMKII (31), would tune the enzyme to a lower ambient Ca level.”
BackgroundPhysiological and Pathological Roles of CaMKII-PP1 Signaling in the Brain
Shioda, N., & Fukunaga, K. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms19010020 · Cited by 76 · see citing works
“However, the composition of the dodecameric CaMKII holoenzyme affects CaMKII localization [78,79].”
BackgroundInitial 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
“, 1994) and form heteromeric holoenzymes in excitatory synapses (Shen et al., 1998; Brocke et al., 1999).”
BackgroundLamsa, K., Irvine, E. E., Giese, K. P., & Kullmann, D. M. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.137380 · Cited by 61 · see citing works
“Indeed, the β subunit is an especially strong candidate since it has been reported to exhibit a higher sensitivity to Ca2+/calmodulin, and to be phosphorylated by the α isoform (Brocke et al. 1999).”
BackgroundFlexible 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 · see citing works
“CaMKII-a and CaMKII-b can assemble into mixed holoenzymes containing both isoforms (Bennett et al., 1983; Brocke et al., 1999; Thiagarajan et al., 2002).”
BackgroundSelf-citationCaMKIIβ 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
“In addition to these differences in susbstrate specificity, the two isoforms have different sensitivities to Ca2+ signals, since the binding affinity for calmodulin is higher for CaMKIIβ homomers than for CaMKIIα homomers [4].”
BackgroundTransient Versus Asymptotic Dynamics of CaM Kinase II: Possible Roles of Phosphatase
Kubota, Y., & Bower, J. M. (2001) · Journal of Computational Neuroscience · doi:10.1023/a:1013727331979 · Cited by 56 · see citing works
“This is an important and well-characterized feature of CaMKII enzyme kinetics (Braun and Schulman, 1995; Hanson and Schulman, 1994; Brocket et al., 1999 ).”
BackgroundResultInfluentialConformational changes underlying calcium/calmodulin‐dependent protein kinase II activation
Hoffman, L., Stein, R. A., Colbran, R. J., & Mchaourab, H. S. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.40 · Cited by 54 · see citing works
“For example, activation properties of CaMKIIb holoenzymes are modulated by the length and sequence of the linker (Brocke et al, 1999; Bayer et al, 2002).”
BackgroundA fresh look at the role of CaMKII in hippocampal synaptic plasticity and memory
Rongo, C. (2002) · BioEssays · doi:10.1002/bies.10057 · Cited by 50 · 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
Activation of the Calcium/Calmodulin-Dependent Protein Kinases as a Consequence of Oxidative Stress
Franklin, R. A., Rodriguez–Mora, O., LaHair, M. M., & McCubrey, J. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1807 · Cited by 47 · see citing works
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 · see citing works
“This result suggests that the ratio of a and b subunits within the same holoenzyme, as found in CaM-kinase II preparations from rat brain (Vallano 1989; Brocke et al. 1999), would in ̄uence their propensity for self-association.”
BackgroundInfluentialBa, M., Kong, M., Yang, H.-Q., Ma, G.-Z., Lu, G.-Q., Chen, S.-D., & Liu, Z.-G. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9177-9 · Cited by 47
“Activation of CaMKII is directly involved in the phosphorylation of AMPA receptor GluR1 subunit serine 831 [15, 16].”
Detailed state model of CaMKII activation and autophosphorylation
Lučić, V., Greif, G. J., & Kennedy, M. B. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0362-4 · Cited by 45 · see citing works
“The affinity of bCaMKII for CaM was in both cases taken to be ten times higher than that of aCaMKII, consistent with the approximately ten times lower EC50 for bCaMKII (Brocke et al. 1999).”
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
“(Brocke et al. 1999), so CaMKIIb expression increases in response to a reduction of neuronal activity, whereas CaMKIIa dominates during elevated levels of neuronal activity (Thiagarajan et al.”
BackgroundInfluentialRegulation 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 · see citing works
“Homomeric CaMKII composed of different isoforms exhibit distinct calmodulin concentration dependences for autophosphorylation, which results from differences in their affinity for calmodulin [ 30 ], and also show significant variations in autophosphorylation rate and substrate phosphorylation [33].”
BackgroundJiao, 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 · see citing works
Novak, G., & Seeman, P. (2010) · Synapse · doi:10.1002/syn.20786 · Cited by 37 · see citing works
“…b will result in phosphorylation of a subunits by a b neighbor at lower Ca21 concentration and a holoenzyme with higher affinity for Ca21/CaM, rendering synapses oversensitive to low Ca21 and easier to trigger (Ahmed et al., 2006; Brocke et al., 1999; Thiagarajan et al., 2002; Ullian et al., 2001).”
BackgroundHosokawa, T., Saito, T., Asada, A., Ohshima, T., Itakura, M., Takahashi, M., Fukunaga, K., & Hisanaga, S. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20975 · Cited by 37
“DOI: 10.1002/jnr.20975 ' 2006 Wiley-Liss, Inc. (Brocke et al., 1999).”
InfluentialCaMK-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 · see citing works
“Integrated with our findings, the observed differences in autophosphorylation [29] could therefore be due to inter-subunit restriction caused by variable domain sequences.”
InfluentialCalcium/calmodulin-dependent protein kinases as potential targets in cancer therapy
Rodriguez–Mora, O., LaHair, M. M., Howe, C. J., McCubrey, J. A., & Franklin, R. A. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.4.791 · Cited by 39 · see citing works
“The product of these genes can be alternatively spliced leading to the production of 24 different polypeptides in vivo [16-19].”
BackgroundBustos, F. J., Jury, N., Martínez, P., Ampuero, E., Campos, M., Abarzúa, S., Jaramillo, K., Ibing, S., Mardones, M. D., Haensgen, H., et al. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25843 · Cited by 35 · see citing works
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 · see citing works
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 · see citing works
Cai, Q., Chen, X., Zhu, S., Nicoll, R. A., & Zhang, M. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112146 · Cited by 31 · see citing works
Hirano, T., & Kawaguchi, S.-Y. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00042 · Cited by 33
“…reported that the relative amounts of α- and β-CaMKII change depending on the neuronal activity and developmental stage in the mammalian central nervous system (Bayer et al., 1999; Thiagarajan et al., 2002). β-CaMKII has much higher affinity to Ca2+/calmodulin than α-CaMKII (Brocke et al., 1999).”
BackgroundDifferential expression of CaMK‐II genes during early zebrafish embryogenesis
Rothschild, S. C., Lister, J. A., & Tombes, R. M. (2006) · Developmental Dynamics · doi:10.1002/dvdy.21005 · Cited by 36 · see citing works
“Six splice variants contain domain I, which is believed to influence CaM binding (Brocke et al., 1999; Bayer et al., 2002).”
BackgroundSeeger, C., Talibov, V., & Danielson, U. H. (2017) · Journal of Molecular Recognition · doi:10.1002/jmr.2621 · Cited by 44 · see citing works
Prediction and validation of a mechanism to control the threshold for inhibitory synaptic plasticity
Kitagawa, Y., Hirano, T., & Kawaguchi, S.-Y. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.39 · Cited by 32 · see citing works
“Taking into consideration the fact that subunits of CaMKII have about 10 times higher affinity to Ca/CaM than subunits (Brocke et al., 1999), the ratio of and subunits of CaMKII might be critical for the threshold control of Ca-mediated CaMKII activation.”
BackgroundBuonarati, O. R., Miller, A. P., Coultrap, S. J., Bayer, K. U., & Reichow, S. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110168 · Cited by 33 · see citing works
“…(as determined by the length of the variable linker region) affects CaM binding: CaMKIIβ is more readily activated by lower concentrations of CaM than the CaMKIIα isoform that has a shorter linker region (Brocke et al., 1999; De Koninck and Schulman, 1998) as also observed in this study.”
BackgroundResultMechanisms 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 · see citing works
Vascular CaMKII: heart and brain in your arteries
Toussaint, F., Charbel, C., Allen, B. G., & Ledoux, J. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00341.2015 · Cited by 29 · see citing works
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 · see citing works
Liu, B., & Neufeld, A. H. (2000) · Glia · doi:10.1002/(sici)1098-1136(200004)30:2 · Cited by 177 · see citing works
Calmodulin-Dependent Protein Kinases
Krebs, J. J. R. (2000) · Springer eBooks · doi:10.1007/978-3-642-58306-3_5 · Cited by 1 · see citing works
Amphetamine sensitization elevates CaMKIIß mRNA
Greenstein, R., Novak, G., & Seeman, P. M. (2007) · Synapse · doi:10.1002/syn.20429 · Cited by 25 · see citing works
“This ratio also regulates the translocation time of the a/b heteromer from F-actin to the postsynaptic density where it phosphorylates its targets (Shen and Meyer, 1999) and also determines the sensitivity of the CaMKII holoenzyme to Ca2þ signals (Brocke et al., 1999).”
BackgroundZheng, 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 29 · see citing works
Anthony, D., Beattie, J., Paul, A., & Currie, S. (2007) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2007.07.003 · Cited by 25
Zemoura, K., Balakrishnan, K. R., Grampp, T., & Benke, D. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1142-5 · Cited by 26 · see citing works
“In brain, CaMKIIα and CaMKIIβ are the predominant subunits and in forebrain neurons the CaMKII holoenzyme largely consists of nine α subunits and three β subunits [37, 38].”
BackgroundShioda, N., Sawai, M., Ishizuka, Y., Shirao, T., & Fukunaga, K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664920 · Cited by 25 · see citing works
“The CaMKII holoenzyme is normally a dodecameric complex formed via isoform variable regions, and its composition affects CaMKII localization (52, 53).”
BackgroundRegulation of gastrointestinal motility by Ca2+/calmodulin-stimulated protein kinase II
Perrino, B. A. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.03.009 · Cited by 18 · see citing works
Neuronal CaMKII acts as a structural kinase
Lin, Y., & Redmond, L. (2009) · Communicative & Integrative Biology · doi:10.4161/cib.2.1.7426 · Cited by 16 · see citing works
Gao, Z., van Woerden, G. M., Elgersma, Y., Zeeuw, C. I. D., & Hoebeek, F. E. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00016 · Cited by 16 · see citing works
“Indeed, we found that in Camk2b−/− Purkinje cells the GABAB-activation was essential to elicit iLTP upon CF stimulation, whereas in Camk2a−/− Purkinje cells GABAB-activation did not trigger iLTP.”
BackgroundResultInfluentialFueta, Y., Fukunaga, K., Ishidao, T., & Hori, H. (2002) · Life Science · doi:10.1016/s0024-3205(02)02247-6 · Cited by 19 · see citing works
Taylor, D. M., Koninck, P. D., Minotti, S., & Durham, H. D. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2006.09.007 · Cited by 18 · see citing works
Murray, K. D., Isackson, P. J., & Jones, E. G. (2003) · Neuroscience · doi:10.1016/j.neuroscience.2003.07.015 · Cited by 18 · see citing works
Savina, T. A., Shchipakina, T., Levin, S. G., & Godukhin, O. V. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.11.023 · Cited by 17 · see citing works
The role of regulatory domain interactions in UNC-43 CaMKII localization and trafficking
Umemura, T., Rapp, P., & Rongo, C. (2005) · Journal of Cell Science · doi:10.1242/jcs.02457 · Cited by 16 · see citing works
“The kinase comprises multiple subunits that associate to form a holoenzyme (Brocke et al., 1999; Gaertner et al., 2004; Hoelz et al., 2003).”
BackgroundSeals, R. C., Urban, R. J., Sekar, N., & Veldhuis, J. D. (2004) · Endocrinology · doi:10.1210/en.2003-1528 · Cited by 18 · see citing works
- Authors
- Brocke, L., Chiang, L. W., Wagner, P. D., & Schulman, H.
- Affiliations
- Stanford Medicine (US)
- National Institutes of Health (US)
- Corresponding author
- Schulman, Howard
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-08
- Volume
- 274
- Issue
- 32
- Pages
- 22713-22722
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2143661877
- Cited by
- 161
- References
- 52
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 3 · 2023: 6 · 2022: 6 · 2021: 3 · 2020: 5 · 2019: 4 · 2018: 7 · 2017: 4 · 2016: 6 · 2015: 4 · 2014: 10 · 2013: 3 · 2012: 5
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5p50mh048108-07)
- National Institute of Mental Health (MH 48108)
- National Institute of General Medical Sciences (GM 30179)
- 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 › Signaling Pathways in Disease
- Keywords
- CaM kinase II, calcium/calmodulin-dependent protein kinase II, subunit composition, alpha and beta subunits, autophosphorylation, hippocampal neurons, calcium oscillations, alternative splicing, forebrain
- MeSH terms
- Animals, Brain, Calcium, Calmodulin, Hippocampus, Isoenzymes, Limbic System, Neurons, Phosphorylation, Precipitin Tests, Protein Binding, RNA, Messenger, Gene Expression, Prosencephalon, Calcium-Calmodulin-Dependent Protein Kinases, Pyramidal Cells, Holoenzymes, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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