Developmental expression of the CaM kinase II isoforms: ubiquitous γ- and δ-CaM kinase II are the early isoforms and most abundant in the developing nervous system

Bayer, K. Ulrich; Löhler, Jürgen; Schulman, Howard; Harbers, Klaus

doi:10.1016/s0169-328x(99)00131-x

Cited by 155 publications

(161 citation statements)

References 32 publications

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“…This may have been represented in our study by the occasional gold particles seen in the cytoplasm but not near the synapse itself. In addition, CaMKIIβ, which is not recognized by our antibody, is very abundant in the brain after birth (mRNA; Bayer et al, 1999), and has been implicated in filopodia extension and synapse formation (Fink et al, 2003). Since CaMKII forms a major portion of the adult PSD, it would not be surprising that similarly structured PSDs at P2 have abundant levels of a developmentally important form of CaMKII, such as CaMKIIβ.…”

Section: Discussionmentioning

confidence: 89%

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Petralia

Sans

Wang

et al. 2005

Molecular and Cellular Neuroscience

209

196

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In glutamatergic synapses, glutamate receptors (GluRs) associate with many other proteins involved in scaffolding and signal transduction. The ontogeny of these postsynaptic density (PSD) proteins involves changes in their composition during development, paralleling changes in GluR type and function. In the CA1 region of the hippocampus, at postnatal day 2 (P2), many synapses already have a distinct PSD. We used immunoblot analysis, subcellular fractionation, and quantitative immunogold electron microscopy to examine the distribution of PSD proteins during development of the hippocampus. Synapses at P2 contained substantial levels of NR1 and NR2B and most GluRassociated proteins, including SAP102, SynGAP, the chain of proteins from GluRs/SAP102 through GKAP/Shank/Homer and metabotropic glutamate receptors, and the adhesion factors, cadherin, catenin, neuroligin, and Nr-CAM. Development was marked by substantial decreases in NR2B and SAP102 and increases in NR2A, PSD-95, AMPA receptors and CaMKII. Other components showed more moderate changes.

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Section: Discussionmentioning

confidence: 89%

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Petralia

Sans

Wang

et al. 2005

Molecular and Cellular Neuroscience

209

196

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“…Whereas GluA2-lacking AMPARs are abundant in early development, GluA2-containing AMPARs dominate in mature synapses (33). Similarly, βCaMKII levels peak earlier in development relative to αCaMKII (34,35). Perhaps AMPAR blockade and activity deprivation cause neurons to revert to an earlier developmental state in which neuronal signaling pathways are geared up for establishing new synaptic connections.…”

Section: Discussionmentioning

confidence: 99%

β Ca ²⁺ /CaM-dependent kinase type II triggers upregulation of GluA1 to coordinate adaptation to synaptic inactivity in hippocampal neurons

Groth

Lindskog

Thiagarajan

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Prolonged AMPA-receptor blockade in hippocampal neuron cultures leads to both an increased expression of GluA1 postsynaptically and an increase in vesicle pool size and turnover rate presynaptically, adaptive changes that extend beyond simple synaptic scaling. As a molecular correlate, expression of the β Ca 2+ /CaM-dependent kinase type II (βCaMKII) is increased in response to synaptic inactivity. Here we set out to clarify the role of βCaMKII in the various manifestations of adaptation. Knockdown of βCaMKII by lentiviral-mediated expression of shRNA prevented the synaptic inactivity-induced increase in GluA1, as did treatment with the CaM kinase inhibitor KN-93, but not the inactive analog KN-92. These results demonstrate that, spurred by AMPA-receptor blockade, up-regulation of βCaMKII promotes increased GluA1 expression. Indeed, transfection of βCaMKII, but not a kinase-dead mutant, increased GluA1 expression on dendrites and elevated vesicle turnover (Syt-Ab uptake), mimicking the effect of synaptic inactivity on both sides of the synapse. In cells with elevated βCaMKII, relief of synaptic-activity blockade uncovered an increase in the frequency of miniature excitatory postsynaptic currents that could be rapidly and fully suppressed by PhTx blockade of GluA1 receptors. This increased mini frequency involved a genuine presynaptic enhancement, not merely an increased abundance of synapses. This finding suggests that Ca 2+ flux through GluA1 receptors may trigger the acute release of a retrograde messenger. Taken together, our results indicate that synaptic inactivity-induced increases in βCaMKII expression set in motion a series of events that culminate in coordinated pre-and postsynaptic adaptations in synaptic transmission.α Ca 2+ /CaM-dependent kinase type II | homeostasis | retrograde signaling | synaptic coordination

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“…Although ␣ and ␤ are the predominant CaMK-II genes transcribed in the central nervous system, ␦ isozymes are the most common CaMK-II gene product in embryonic cells (6,8,10,12). Mouse embryonic cells express some ␤ e , ␥ C , and ␥ B gene products but primarily express ␦ C CaMK-II (12,21,23).…”

mentioning

confidence: 99%

Cytosolic Targeting Domains of γ and δ Calmodulin-dependent Protein Kinase II

Caran

Johnson

Jenkins

et al. 2001

Journal of Biological Chemistry

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Ca2؉ /calmodulin-dependent protein kinase II (CaMK-II) isozyme variability is the result of alternative usage of variable domain sequences. Isozyme expression is cell type-specific to transduce the appropriate Ca 2؉ signals. We have determined the subcellular targeting domain of ␦ E CaMK-II, an isozyme that induces neurite outgrowth, and of a structurally similar isozyme, ␥ C CaMK-II, which does not induce neurite outgrowth. ␦ E CaMK-II co-localizes with filamentous actin in the perinuclear region and in cellular extensions. In contrast, ␥ C CaMK-II is uniformly cytosolic. Constitutively active ␦ E CaMK-II induces F-actin-rich extensions, thereby supporting a functional role for its localization. C-terminal constructs, which lack central variable domain sequences, can oligomerize and localize like full-length ␦ E and ␥ C CaMK-II. Central variable domains themselves are monomeric and have no targeting capability. The C-terminal 95 residues of ␦ CaMK-II also has no targeting capability but can efficiently oligomerize. These findings define a targeting domain for ␥ and ␦ CaMK-IIs that is in between the central variable and association domains. This domain is responsible for the subcellular targeting differences between ␥ and ␦ CaMK-IIs.

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Developmental expression of the CaM kinase II isoforms: ubiquitous γ- and δ-CaM kinase II are the early isoforms and most abundant in the developing nervous system

Cited by 155 publications

References 32 publications

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Ontogeny of postsynaptic density proteins at glutamatergic synapses

β Ca ²⁺ /CaM-dependent kinase type II triggers upregulation of GluA1 to coordinate adaptation to synaptic inactivity in hippocampal neurons

Cytosolic Targeting Domains of γ and δ Calmodulin-dependent Protein Kinase II

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Developmental expression of the CaM kinase II isoforms: ubiquitous γ- and δ-CaM kinase II are the early isoforms and most abundant in the developing nervous system

Cited by 155 publications

References 32 publications

Ontogeny of postsynaptic density proteins at glutamatergic synapses

Ontogeny of postsynaptic density proteins at glutamatergic synapses

β Ca 2+ /CaM-dependent kinase type II triggers upregulation of GluA1 to coordinate adaptation to synaptic inactivity in hippocampal neurons

Cytosolic Targeting Domains of γ and δ Calmodulin-dependent Protein Kinase II

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β Ca ²⁺ /CaM-dependent kinase type II triggers upregulation of GluA1 to coordinate adaptation to synaptic inactivity in hippocampal neurons