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dc.contributor.authorMyrum, Craigen_US
dc.contributor.authorSoule, Jonathanen_US
dc.contributor.authorBittins, Margaretheen_US
dc.contributor.authorCavagnini, Kyleen_US
dc.contributor.authorGoff, Kevinen_US
dc.contributor.authorZiemek, Silje Karinaen_US
dc.contributor.authorEriksen, Maria Steeneen_US
dc.contributor.authorPatil, Sudarshanen_US
dc.contributor.authorSzum, Adrianen_US
dc.contributor.authorNair Raveendran, Rajeevkumaren_US
dc.contributor.authorBramham, Clive R.en_US
dc.date.accessioned2018-08-10T13:07:12Z
dc.date.available2018-08-10T13:07:12Z
dc.date.issued2017-09-20
dc.PublishedMyrum C, Soule J, Bittins M, Cavagnini, Goff, Ziemek, Eriksen MS, Patil S, Szum, Nair Raveendran R, Bramham CRE. Arc interacts with the integral endoplasmic reticulum protein, calnexin. Frontiers in Cellular Neuroscience. 2017;11:294eng
dc.identifier.issn1662-5102
dc.identifier.urihttps://hdl.handle.net/1956/18041
dc.description.abstractActivity-regulated cytoskeleton-associated protein, Arc, is a major regulator of long-term synaptic plasticity and memory formation. Here we reveal a novel interaction partner of Arc, a resident endoplasmic reticulum transmembrane protein, calnexin. We show an interaction between recombinantly-expressed GST-tagged Arc and endogenous calnexin in HEK293, SH-SY5Y neuroblastoma and PC12 cells. The interaction was dependent on the central linker region of the Arc protein that is also required for endocytosis of AMPA-type glutamate receptors. High-resolution proximity-ligation assays (PLAs) demonstrate molecular proximity of endogenous Arc with the cytosolic C-terminus, but not the lumenal N-terminus of calnexin. In hippocampal neuronal cultures treated with brain-derived neurotrophic factor (BDNF), Arc interacted with calnexin in the perinuclear cytoplasm and dendritic shaft. Arc also interacted with C-terminal calnexin in the adult rat dentate gyrus (DG). After induction of long-term potentiation (LTP) in the perforant path projection to the DG of adult anesthetized rats, enhanced interaction between Arc and calnexin was obtained in the dentate granule cell layer (GCL). Although Arc and calnexin are both implicated in the regulation of receptor endocytosis, no modulation of endocytosis was detected in transferrin uptake assays. Previous work showed that Arc interacts with multiple protein partners to regulate synaptic transmission and nuclear signaling. The identification of calnexin as a binding partner further supports the role of Arc as a hub protein and extends the range of Arc function to the endoplasmic reticulum, though the function of the Arc/calnexin interaction remains to be defined.en_US
dc.language.isoengeng
dc.publisherFrontierseng
dc.rightsAttribution CC BYeng
dc.rights.urihttp://creativecommons.org/licenses/by/4.0eng
dc.subjectarceng
dc.subjectcalnexineng
dc.subjectendoplasmic reticulumeng
dc.subjectproximity ligation assayeng
dc.subjectendocytosiseng
dc.subjectsynaptic plasticityeng
dc.titleArc interacts with the integral endoplasmic reticulum protein, calnexinen_US
dc.typePeer reviewed
dc.typeJournal article
dc.date.updated2018-03-06T13:24:35Z
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2017 The Author(s)
dc.identifier.doihttps://doi.org/10.3389/fncel.2017.00294
dc.identifier.cristin1517671
dc.source.journalFrontiers in Cellular Neuroscience


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