Activity-driven postsynaptic translocation of CaMKII

Merrill, Michelle A.; Chen, Yucui; Strack, Stefan; Hell, Johannes

doi:10.1016/j.tips.2005.10.003

Cited by 138 publications

(152 citation statements)

References 79 publications

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“…Numerous studies have shown that strong synaptic activation results in an increase in binding of the kinase to NMDAR (Colbran, 2004;Schulman, 2004;Merrill et al, 2005). Using fluorescent imaging in living cells, we demonstrated previously that the amount of bound CaMKII␣ in spines persistently increases after induction of LTP (Otmakhov et al, 2004).…”

Section: Introductionmentioning

confidence: 70%

“…One of the main postsynaptic binding partners of CaMKII at the synapse is the NMDA receptor (Colbran, 2004;Schulman, 2004;Merrill et al, 2005). Labeling studies indicate that the number of NMDARs at individual synapses weakly but significantly correlates with synapse size (Racca et al, 2000), suggesting that CaMKII binding to NMDAR could contribute to the correlation we observe, although kinase self-association or binding to other PSD targets may also be a participating factor.…”

Section: Camkii Content and Spine Sizementioning

confidence: 75%

“…This large amount of the kinase has suggested that CaMKII has a structural role at synapses in addition to its enzymatic role (Erondu and Kennedy, 1985). Indeed, CaMKII holoenzymes are capable of self-association and can bind to multiple spine proteins, including NMDA receptors (NMDARs) in the PSD and F-actin in the spine head (Kennedy, 1998;Colbran, 2004;Schulman, 2004;Merrill et al, 2005). Notably, binding to the NMDAR is required for regulating synaptic strength (Barria and Malinow, 2005) and binding to F-actin has been implicated in controlling spine morphogenesis (Fink et al, 2003;Narayanan et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…CaMKII enrichment at synapses is regulated by synaptic activity (Meyer and Shen, 2000;Colbran, 2004;Schulman, 2004;Merrill et al, 2005). Numerous studies have shown that strong synaptic activation results in an increase in binding of the kinase to NMDAR (Colbran, 2004;Schulman, 2004;Merrill et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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Synaptic Strength of Individual Spines Correlates with Bound Ca²⁺–Calmodulin-Dependent Kinase II

Asrican¹,

Lisman²,

Otmakhov³

2007

J. Neurosci.

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Both synaptic strength and spine size vary from spine to spine, but are strongly correlated. This gradation is regulated by activity and may underlie information storage. Ca 2ϩ -calmodulin-dependent kinase II (CaMKII) is critically involved in the regulation of synaptic strength and spine size. The high amount of the kinase in the postsynaptic density has suggested that the kinase has a structural role at synapses. We demonstrated previously that the bound amount of CaMKII␣ in spines persistently increases after induction of long-term potentiation, prompting the hypothesis that this amount may correlate with synaptic strength. To test this hypothesis we combined two recently developed methods, two-photon uncaging of glutamate for determining the EPSC of individual spines (uEPSC) and quantitative microscopy for measuring bound CaMKII␣ in the same spines. We found that under basal conditions the relative bound amount of CaMKII␣ varied over a 10-fold range and positively correlated with the uEPSC. Both the bound amount of CaMKII␣ in spines and uEPSC also positively correlated with spine size. Interestingly, the bound CaMKII␣ fraction (bound/total CaMKII␣ in spines) remained remarkably constant across all spines. The results are consistent with the hypothesis that bound CaMKII serves as a structural organizer of postsynaptic molecules and thereby may be involved in maintaining spine size and synaptic strength.

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Section: Introductionmentioning

confidence: 70%

Section: Camkii Content and Spine Sizementioning

confidence: 75%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Synaptic Strength of Individual Spines Correlates with Bound Ca²⁺–Calmodulin-Dependent Kinase II

Asrican¹,

Lisman²,

Otmakhov³

2007

J. Neurosci.

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“…This inter-subunit phosphorylation of Thr-286/287 converts the kinase into a high affinity binding protein for Ca 2ϩ /CaM, and the kinase becomes an activatorindependent autonomous enzyme (3). The autophosphorylation also leads to increased affinity of the kinase for several proteins near the sites of elevated Ca 2ϩ with functional consequences (4,5).…”

mentioning

confidence: 99%

Ischemia-elicited Oxidative Modulation of Ca2+/Calmodulin-dependent Protein Kinase II

Shetty

Huang

2008

Journal of Biological Chemistry

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Ca 2؉ /calmodulin (CaM)-dependent protein kinase II (CaMKII) plays a critical role in neuronal signal transduction and synaptic plasticity. Here, we showed that this kinase was very susceptible to oxidative modulation. Treatment of mouse brain synaptosomes with H 2 O 2 , diamide, and sodium nitroprusside caused aggregation of CaMKII through formation of disulfide and non-disulfide linkages, and partial inhibition of the kinase activity. These CaMKII aggregates were found to associate with the post synaptic density. However, treatment of purified CaMKII with these oxidants did not replicate those effects observed in the synaptosomes. Using two previously identified potential mediators of oxidants in the brain, glutathione disulfide S-monoxide (GS-DSMO) and glutathione disulfide S-dioxide (GS-DSDO), we showed that they oxidized and inhibited CaMKII in a manner partly related to those of the oxidanttreated synaptosomes as well as the ischemia-elicited oxidative stress in the acutely prepared hippocampal slices. Interestingly, the autophosphorylated and activated CaMKII was relatively refractory to GS-DSMO-and GS-DSDO-mediated aggregation. Short term ischemia (10 min) caused a depression of basal synaptic response of the hippocampal slices, and re-oxygenation (after 10 min) reversed the depression. However, oxidation of CaMKII remained at above the pre-ischemic level throughout the treatment. Oxidation of CaMKII also prevented full recovery of CaMKII autophosphorylation after re-oxygenation. Subsequently, the high frequency stimulation-mediated synaptic potentiation in the hippocampal CA1 region was significantly reduced compared with the control without ischemia. Thus, ischemia-evoked oxidation of CaMKII, probably via the action of glutathione disulfide S-oxides or their analogues, may be involved in the suppression of synaptic plasticity.Ca 2ϩ /calmodulin (CaM) 2 -dependent protein kinase II (CaMKII) is one of the major Ca 2ϩ -sensing enzymes important in transducing neuronal, hormonal, and electrical signals in brain, heart, and other tissues. In the central nervous system, CaMKII plays a pivotal role in the facilitation of synaptic plasticity, learning, and memory and in activity-dependent developmental processes (1). CaMKII holoenzyme is a dodecamer composed of two stacked hexameric rings, in which each catalytic/regulatory domain from the upper ring interacts with the equivalent catalytic/regulatory domain in the lower ring by an antiparallel coiled-coil, which resides in regulatory domains (2). Binding of Ca 2ϩ /CaM to the regulatory domain separates the dimer pair and causes the exposure of Thr-286 or Thr-287 (within ␣ or ␤ subunit) for phosphorylation by another catalytic domain in the same ring. This inter-subunit phosphorylation of Thr-286/287 converts the kinase into a high affinity binding protein for Ca 2ϩ /CaM, and the kinase becomes an activatorindependent autonomous enzyme (3). The autophosphorylation also leads to increased affinity of the kinase for several proteins near the sites of elevated Ca 2...

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Sperm and oocyte communication mechanisms controlling C. elegans fertility

Han

Cottee

Miller

2009

Developmental Dynamics

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During sexual reproduction in many species, sperm and oocyte secrete diffusible signaling molecules to help orchestrate the biological symphony of fertilization. In the Caenorhabditis elegans gonad, bidirectional signaling between sperm and oocyte is important for guiding sperm to the fertilization site and inducing oocyte maturation. The molecular mechanisms that regulate sperm guidance and oocyte maturation are being delineated. Unexpectedly, these mechanisms are providing insight into human diseases, such as amyotrophic lateral sclerosis, spinal muscular atrophy, and cancer. Here we review sperm and oocyte communication in C. elegans and discuss relationships to human disorders. Developmental Dynamics 239:1265-1281,

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Activity-driven postsynaptic translocation of CaMKII

Cited by 138 publications

References 79 publications

Synaptic Strength of Individual Spines Correlates with Bound Ca²⁺–Calmodulin-Dependent Kinase II

Synaptic Strength of Individual Spines Correlates with Bound Ca²⁺–Calmodulin-Dependent Kinase II

Ischemia-elicited Oxidative Modulation of Ca2+/Calmodulin-dependent Protein Kinase II

Sperm and oocyte communication mechanisms controlling C. elegans fertility

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Activity-driven postsynaptic translocation of CaMKII

Cited by 138 publications

References 79 publications

Synaptic Strength of Individual Spines Correlates with Bound Ca2+–Calmodulin-Dependent Kinase II

Synaptic Strength of Individual Spines Correlates with Bound Ca2+–Calmodulin-Dependent Kinase II

Ischemia-elicited Oxidative Modulation of Ca2+/Calmodulin-dependent Protein Kinase II

Sperm and oocyte communication mechanisms controlling C. elegans fertility

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Product

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Synaptic Strength of Individual Spines Correlates with Bound Ca²⁺–Calmodulin-Dependent Kinase II

Synaptic Strength of Individual Spines Correlates with Bound Ca²⁺–Calmodulin-Dependent Kinase II