<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" altimg="si5.gif" display="inline" overflow="scroll"><mml:mi>m</mml:mi></mml:math>-dominating <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" altimg="si6.gif" display="inline" overflow="scroll"><mml:mi>k</mml:mi></mml:math>-ended trees of graphs

Kanō, Mikio; Tsugaki, Masao; Yan, Guangwu

doi:10.1016/j.disc.2014.06.005

Cited by 6 publications

(11 citation statements)

References 3 publications

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“…This RP induction was suppressed by inhibition of CaMKII activity using a specific inhibitor AIPII (1 μM) (100 ± 14%, P < 0.05 compared with control). Thus, in accordance with previous studies (Kano et al 1996;Kawaguchi & Hirano, 2002), CaMKII activity is essential for RP induction.…”

Section: Expression Of αAnd βCamkii In a Pnsupporting

confidence: 93%

“…Considering the direct potentiating effect of GABA A R phosphorylation by CaMKII (Houston & Smart, 2006;Houston et al 2008), sustained CaMKII activity is a potential mechanism for expression and maintenance of RP. However, KN62 treatment after RP induction was previously shown to have little effect on the once-established RP in a slice preparation (Kano et al 1996). Consistently, our preliminary data suggested that RP was not cancelled by CaMKII inhibition from 5 min after the induction (data not shown).…”

Section: Sustained Camkii Activation and Synaptic Plasticitysupporting

confidence: 84%

“…Previous immunocytochemical studies showed that the sustained autophosphorylation of CaMKII at Thr286/287 takes place for longer than 2 h upon transient high K + treatment of cultured PNs (Kitagawa et al 2009). Direct application of pre-activated (Thr286-phosphorylated) αCaMKII was shown to induce RP by itself (Kano et al 1996). Considering the direct potentiating effect of GABA A R phosphorylation by CaMKII (Houston & Smart, 2006;Houston et al 2008), sustained CaMKII activity is a potential mechanism for expression and maintenance of RP.…”

Section: Sustained Camkii Activation and Synaptic Plasticitymentioning

confidence: 99%

“…This inhibitory synaptic LTP induced by heterosynaptic excitatory inputs is called rebound potentiation (RP). Distinct from NMDA receptor-dependent LTP at excitatory synapses, RP induction depends on the Ca 2+ influx through voltage-gated Ca 2+ channels and the resultant activation of CaMKII (Kano et al 1996). CaMKII was shown to directly phosphorylate GABA A Rs augmenting the channel currents (Houston & Smart, 2006;Houston et al 2008), although the roles of the direct phosphorylation in RP remain elusive.…”

Section: Introductionmentioning

confidence: 99%

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Opposite regulation of inhibitory synaptic plasticity by α and β subunits of Ca²⁺/calmodulin‐dependent protein kinase II

Nagasaki

Hirano

Kawaguchi

2014

The Journal of Physiology

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Key pointsr At inhibitory synapses on a cerebellar Purkinje neuron, depolarization-caused Ca 2+ increase induces long-term potentiation (known as rebound potentiation, RP).r We show that the subunit composition of a Ca 2+ /calmodulin-dependent protein kinase II (CaMKII) holoenzyme, consisting of α-and βCaMKII, is critical for RP induction.r βCaMKII plays an essential role in RP induction depending on the high affinity for Ca 2+ /CaM but not on the F-actin-binding property, whereas αCaMKII negatively regulates it.r βCaMKII enrichment prolongs total CaMKII activation depending on Thr286/287 autophosphorylation.r α-and βCaMKII expression ratio might play critical roles in regulation of synaptic functions in the central nervous system. Abstract Induction of several forms of synaptic plasticity, a cellular basis for learning and memory, depends on the activation of Ca 2+ /calmodulin (CaM)-dependent protein kinase II (CaMKII). CaMKII acts as a holoenzyme consisting of α and β subunits (α-and βCaMKII). However, it remains elusive how the subunit composition of a CaMKII holoenzyme affects its activation and hence synaptic plasticity. We addressed this issue by focusing on long-term potentiation (LTP) at inhibitory synapses on cerebellar Purkinje neurons (PNs) (called rebound potentiation, RP). The contribution of each subunit to RP was examined by selective knock-down or overexpression of that subunit. Electrophysiological recording from a rat cultured PN demonstrated that βCaMKII is essential for RP induction, whereas αCaMKII suppresses it. Thus, RP was negatively regulated due to the greater relative abundance of αCaMKII compared to βCaMKII, suggesting a critical role of CaMKII subunit composition in RP. The higher affinity of βCaMKII to Ca 2+ /CaM compared with αCaMKII was responsible for the predominant role in RP induction. Live-cell imaging of CaMKII activity based on the Förster resonance energy transfer (FRET) technique revealed that βCaMKII enrichment enhances the total CaMKII activation upon a transient conditioning depolarization. Taken together, these findings clarified that α-and βCaMKII oppositely regulate CaMKII activation, controlling the induction of inhibitory synaptic plasticity in a PN, which might contribute to the adaptive information processing of the cerebellar cortex.

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Section: Expression Of αAnd βCamkii In a Pnsupporting

confidence: 93%

Section: Sustained Camkii Activation and Synaptic Plasticitysupporting

confidence: 84%

Section: Sustained Camkii Activation and Synaptic Plasticitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Opposite regulation of inhibitory synaptic plasticity by α and β subunits of Ca²⁺/calmodulin‐dependent protein kinase II

Nagasaki

Hirano

Kawaguchi

2014

The Journal of Physiology

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“…[1,2] Soft sensor is an effective approach to cope with this issue. [3,4] It is actually a predictive mathematical model describing the underlying mapping relationship between the secondary variable and the primary variable. [5,6] Such predictive model is realized in computer programs.…”

Section: Introductionmentioning

confidence: 99%

Soft sensor development for nonlinear and time‐varying processes based on supervised ensemble learning with improved process state partition

Shao

Tian

Wang

2015

Asia-Pacific J Chem Eng

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The nonlinearities and time‐varying characteristics are two major causes of low performance of soft sensors in process systems. Motivated of solving the two problems, this paper proposes an adaptive soft sensing method under the ensemble learning framework. An improved process state partition scheme is proposed to construct independent local models, which not only inherits the merits of the original process state partition method but also possesses the function of detecting and deleting redundant models. These prepared local models are weighted by a supervised weighting mechanism and then combined via the Bayesian inference to predict the y‐value of the query sample. Because the weighting mechanism can fully exploit the historical data set and quantify each local model's generalization ability for the query sample, it is potential to compute the combination weights more accurately. Simulations are conducted on two benchmark data sets from two real‐life chemical processes. Extensive performance evaluations of the proposed soft sensor are conducted, and results show its effectiveness. © 2015 Curtin University of Technology and John Wiley & Sons, Ltd.

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m-dominating k-ended trees of l-connected graphs

Tsugaki

Yan

2017

AKCE International Journal of Graphs and Combinatorics

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m-dominating k-ended trees of graphs

Cited by 6 publications

References 3 publications

Opposite regulation of inhibitory synaptic plasticity by α and β subunits of Ca²⁺/calmodulin‐dependent protein kinase II

Opposite regulation of inhibitory synaptic plasticity by α and β subunits of Ca²⁺/calmodulin‐dependent protein kinase II

Soft sensor development for nonlinear and time‐varying processes based on supervised ensemble learning with improved process state partition

m-dominating k-ended trees of l-connected graphs

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m-dominating k-ended trees of graphs

Cited by 6 publications

References 3 publications

Opposite regulation of inhibitory synaptic plasticity by α and β subunits of Ca2+/calmodulin‐dependent protein kinase II

Opposite regulation of inhibitory synaptic plasticity by α and β subunits of Ca2+/calmodulin‐dependent protein kinase II

Soft sensor development for nonlinear and time‐varying processes based on supervised ensemble learning with improved process state partition

m-dominating k-ended trees of l-connected graphs

Contact Info

Product

Resources

About

Opposite regulation of inhibitory synaptic plasticity by α and β subunits of Ca²⁺/calmodulin‐dependent protein kinase II

Opposite regulation of inhibitory synaptic plasticity by α and β subunits of Ca²⁺/calmodulin‐dependent protein kinase II