Regulation of Calcium/Calmodulin-dependent Protein Kinase II Docking toN-Methyl-d-aspartate Receptors by Calcium/Calmodulin and α-Actinin

Leonard, A. Soren; Bayer, K. Ulrich; Merrill, Michelle A.; Lim, Indra A.; Shea, Madeline A.; Schulman, Howard; Hell, Johannes

doi:10.1074/jbc.m205164200

Cited by 129 publications

(176 citation statements)

References 42 publications

(107 reference statements)

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“…In addition, T286 phosphorylation has been shown to decrease the dissociation rate of the kinase from the PSD (Shen et al, 2000;Bayer et al, 2006;Yoshimura and Yamauchi, 1997;Dosemeci et al, 2002). It has also been observed that autophosphorylation of T305/6 inhibits binding of αCaMKII to the PSD and several PSD proteins (Strack et al, 1997b;Leonard et al, 2002;Robison et al, 2005). Furthermore, it has been demonstrated that T305/6 phosphorylation increases the dissociation rate of the kinase from the PSD (Shen et al, 2000).…”

Section: Discussionmentioning

confidence: 97%

“…Several studies have indicated that αCaMKII autophosphorylation of T286 enhances binding of the kinase to the PSD and several of its constituents (Bayer et al, 2001;Strack et al, 1997b;Strack and Colbran, 1998;Gardoni et al, 1999;Leonard et al, 2002;Strack et al, 2000). In addition, T286 phosphorylation has been shown to decrease the dissociation rate of the kinase from the PSD (Shen et al, 2000;Bayer et al, 2006;Yoshimura and Yamauchi, 1997;Dosemeci et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

“…Aside from promoting Ca 2+ -independent activity of CaMKII, T286 phosphorylation has also been shown to regulate its protein-protein interactions. Phosphorylation of this residue is thought to enhance CaMKII binding to isolated PSDs (Strack et al, 1997b), densin-180 (Strack et al, 2000), and the Nmethyl-D-aspartate receptor (NMDAR) subunits NR2B (Strack and Colbran, 1998;Bayer et al, 2001;Leonard et al, 2002), NR1 (Leonard et al, 2002), and NR2A (Gardoni et al, 1999). Furthermore, T286 phosphorylation has been reported to decrease the dissociation rate of CaMKII that has been bound to the PSD (Shen et al, 2000;Bayer et al, 2006;Yoshimura and Yamauchi, 1997;Dosemeci et al, 2002) (but see (Strack et al, 1997b)).…”

Section: Introductionmentioning

confidence: 99%

“…Like T286 phosphorylation, T305/6 phosphorylation has been shown to modulate protein-protein interactions of CaMKII. Phosphorylation of these residues inhibits kinase binding to isolated PSDs (Strack et al, 1997b), α-actinin (Robison et al, 2005), and the NMDAR subunits NR1 and NR2B (Leonard et al, 2002). In addition, T305/6 phosphorylation increases the dissociation rate of CaMKII from the PSD (Shen et al, 2000), and mimicking phosphorylation on these residues prevents while inhibiting phosphorylation enhances PSD association of the kinase (Elgersma et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

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αCaMKII autophosphorylation levels differ depending on subcellular localization

et al. 2007

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Calcium/calmodulin-dependent protein kinase II (CaMKII) has important roles in many processes in the central nervous system. It is enriched at the post-synaptic density (PSD), a localization which is thought to be critical for many of its proposed neuronal functions. In order to better understand the mechanisms that regulate association of CaMKII with the PSD, we compared the levels of autophosphorylation between PSD-associated kinase and kinase in other parts of the neuron. We were surprised to find that αCaMKII in a PSD-enriched fraction prepared from recovered hippocampal CA1-minislices had a relatively low level of threonine 286 (T286) phosphorylation and a relatively high level of threonine 305 (T305) phosphorylation. Furthermore, when the minislices were subjected to a treatment that mimics ischemic conditions, there was a significant translocation of αCaMKII to the PSD-enriched fraction accompanied with a dramatic reduction in T286 phosphorylation levels throughout the neuron. These findings have important implications for our understanding of the role of autophosphorylation in the localization of CaMKII.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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αCaMKII autophosphorylation levels differ depending on subcellular localization

et al. 2007

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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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Role of densin‐180 in mouse ventral hippocampal neurons in 24‐hr retention of contextual fear conditioning

Kim

et al. 2020

Brain and Behavior

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Regulation of Calcium/Calmodulin-dependent Protein Kinase II Docking toN-Methyl-d-aspartate Receptors by Calcium/Calmodulin and α-Actinin

Cited by 129 publications

References 42 publications

αCaMKII autophosphorylation levels differ depending on subcellular localization

αCaMKII autophosphorylation levels differ depending on subcellular localization

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

Role of densin‐180 in mouse ventral hippocampal neurons in 24‐hr retention of contextual fear conditioning

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