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Conference Paper: APCCdh1 mediates EphA4-dependent downregulation of AMPA receptors in homeostatic plasticity

TitleAPCCdh1 mediates EphA4-dependent downregulation of AMPA receptors in homeostatic plasticity
Authors
Issue Date2011
Citation
Nature Neuroscience, 2011, v. 14 n. 2, p. 181-191 How to Cite?
AbstractHomeostatic plasticity is crucial for maintaining neuronal output by counteracting unrestrained changes in synaptic strength. Chronic elevation of synaptic activity by bicuculline reduces the amplitude of miniature excitatory postsynaptic currents (mEPSCs), but the underlying mechanisms of this effect remain unclear. We found that activation of EphA4 resulted in a decrease in synaptic and surface GluR1 and attenuated mEPSC amplitude through a degradation pathway that requires the ubiquitin proteasome system (UPS). Elevated synaptic activity resulted in increased tyrosine phosphorylation of EphA4, which associated with the ubiquitin ligase anaphase-promoting complex (APC) and its activator Cdh1 in neurons in a ligand-dependent manner. APCCdh1 interacted with and targeted GluR1 for proteasomal degradation in vitro, whereas depletion of Cdh1 in neurons abolished the EphA4-dependent downregulation of GluR1. Knockdown of EphA4 or Cdh1 prevented the reduction in mEPSC amplitude in neurons that was a result of chronic elevated activity. Our results define a mechanism by which EphA4 regulates homeostatic plasticity through an APC Cdh1-dependent degradation pathway. © 2011 Nature America, Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/196718
ISSN
2015 Impact Factor: 16.724
2015 SCImago Journal Rankings: 13.558
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorFu, AKY-
dc.contributor.authorHung, K-W-
dc.contributor.authorFu, W-Y-
dc.contributor.authorShen, C-
dc.contributor.authorChen, Y-
dc.contributor.authorXia, J-
dc.contributor.authorLai, K-O-
dc.contributor.authorIp, NY-
dc.date.accessioned2014-04-24T02:10:36Z-
dc.date.available2014-04-24T02:10:36Z-
dc.date.issued2011-
dc.identifier.citationNature Neuroscience, 2011, v. 14 n. 2, p. 181-191-
dc.identifier.issn1097-6256-
dc.identifier.urihttp://hdl.handle.net/10722/196718-
dc.description.abstractHomeostatic plasticity is crucial for maintaining neuronal output by counteracting unrestrained changes in synaptic strength. Chronic elevation of synaptic activity by bicuculline reduces the amplitude of miniature excitatory postsynaptic currents (mEPSCs), but the underlying mechanisms of this effect remain unclear. We found that activation of EphA4 resulted in a decrease in synaptic and surface GluR1 and attenuated mEPSC amplitude through a degradation pathway that requires the ubiquitin proteasome system (UPS). Elevated synaptic activity resulted in increased tyrosine phosphorylation of EphA4, which associated with the ubiquitin ligase anaphase-promoting complex (APC) and its activator Cdh1 in neurons in a ligand-dependent manner. APCCdh1 interacted with and targeted GluR1 for proteasomal degradation in vitro, whereas depletion of Cdh1 in neurons abolished the EphA4-dependent downregulation of GluR1. Knockdown of EphA4 or Cdh1 prevented the reduction in mEPSC amplitude in neurons that was a result of chronic elevated activity. Our results define a mechanism by which EphA4 regulates homeostatic plasticity through an APC Cdh1-dependent degradation pathway. © 2011 Nature America, Inc. All rights reserved.-
dc.languageeng-
dc.relation.ispartofNature Neuroscience-
dc.titleAPCCdh1 mediates EphA4-dependent downregulation of AMPA receptors in homeostatic plasticity-
dc.typeConference_Paper-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/nn.2715-
dc.identifier.pmid21186356-
dc.identifier.scopuseid_2-s2.0-79251584863-
dc.identifier.volume14-
dc.identifier.issue2-
dc.identifier.spage181-
dc.identifier.epage191-
dc.identifier.isiWOS:000286595400015-

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