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Myrum C, Soulé J, Bittins M, et al. Arc Interacts with the Integral Endoplasmic Reticulum Protein, Calnexin. Front Cell Neurosci. 2017;11:294doi: 10.3389/fncel.2017.00294.
Myrum, C., Soulé, J., Bittins, M., Cavagnini, K., Goff, K., Ziemek, S. K., Eriksen, M. S., Patil, S., Szum, A., Nair, R. R., & Bramham, C. R. (2017). Arc Interacts with the Integral Endoplasmic Reticulum Protein, Calnexin. Frontiers in cellular neuroscience, 11294. https://doi.org/10.3389/fncel.2017.00294
Myrum, Craig, et al. "Arc Interacts with the Integral Endoplasmic Reticulum Protein, Calnexin." Frontiers in cellular neuroscience vol. 11 (2017): 294. doi: https://doi.org/10.3389/fncel.2017.00294
Myrum C, Soulé J, Bittins M, Cavagnini K, Goff K, Ziemek SK, Eriksen MS, Patil S, Szum A, Nair RR, Bramham CR. Arc Interacts with the Integral Endoplasmic Reticulum Protein, Calnexin. Front Cell Neurosci. 2017 Sep 20;11:294. doi: 10.3389/fncel.2017.00294. eCollection 2017. PMID: 28979192; PMCID: PMC5611444.
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Front Cell Neurosci. 2017 Sep 20;11:294. doi: 10.3389/fncel.2017.00294. eCollection 2017.

Arc Interacts with the Integral Endoplasmic Reticulum Protein, Calnexin.

Frontiers in cellular neuroscience

Craig Myrum, Jonathan Soulé, Margarethe Bittins, Kyle Cavagnini, Kevin Goff, Silje K Ziemek, Maria S Eriksen, Sudarshan Patil, Adrian Szum, Rajeevkumar R Nair, Clive R Bramham

Affiliations

  1. Dr. Einar Martens Research Group for Biological Psychiatry, Center for Medical Genetics and Molecular Medicine, Haukeland University HospitalBergen, Norway.
  2. Department of Biomedicine and the K.G. Jebsen Center for Research on Neuropsychiatric Disorders, University of BergenBergen, Norway.

PMID: 28979192 PMCID: PMC5611444 DOI: 10.3389/fncel.2017.00294

Abstract

Activity-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.

Keywords: arc; calnexin; endocytosis; endoplasmic reticulum; proximity ligation assay; synaptic plasticity

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