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      Activity-dependent decrease in contact areas between subsurface cisterns and plasma membrane of hippocampal neurons

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      Author(s):
      Publication date (Electronic):
      Journal: Molecular Brain
      Publisher: BioMed Central
      Keywords: ER-PM contact sites, Calcium regulation, Electron microscopy

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          Abstract

          Subsurface cistern (SSC) in neuronal soma and primary dendrites is a specialized compartment of endoplasmic reticulum (ER) that is in close apposition (10 nm) with the plasma membrane (PM). ER-PM contact areas are thought to be involved in intracellular calcium regulation. Here, structural changes of SSC in hippocampal neurons were examined by electron microscopy upon depolarization with high K + (90 mM) or application of NMDA (50 μM) in rat dissociated cultures as well as organotypic slice cultures. The number and average length of SSC-PM contact areas in neuronal somas significantly decreased within 30 s under excitatory condition. This decrease in SSC-PM contact area progressed with time and was reversible. These results demonstrate a structural decoupling between the SSC and the PM upon stimulation, suggesting that there may be a functional decoupling of the calcium regulation. Because SSC-PM contact areas may mediate calcium influx, the decrease in contact area may protect neurons from calcium overload upon heightened stimulation.

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          The online version of this article (10.1186/s13041-018-0366-7) contains supplementary material, which is available to authorized users.

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          PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins.

          Francesca Giordano, Yasunori Saheki, Olof Idevall-Hagren … (2013)
          Most available information on endoplasmic reticulum (ER)-plasma membrane (PM) contacts in cells of higher eukaryotes concerns proteins implicated in the regulation of Ca(2+) entry. However, growing evidence suggests that such contacts play more general roles in cell physiology, pointing to the existence of additionally ubiquitously expressed ER-PM tethers. Here, we show that the three extended synaptotagmins (E-Syts) are ER proteins that participate in such tethering function via C2 domain-dependent interactions with the PM that require PI(4,5)P2 in the case of E-Syt2 and E-Syt3 and also elevation of cytosolic Ca(2+) in the case of E-Syt1. As they form heteromeric complexes, the E-Syts confer cytosolic Ca(2+) regulation to ER-PM contact formation. E-Syts-dependent contacts, however, are not required for store-operated Ca(2+) entry. Thus, the ER-PM tethering function of the E-Syts (tricalbins in yeast) mediates the formation of ER-PM contacts sites, which are functionally distinct from those mediated by STIM1 and Orai1. Copyright © 2013 Elsevier Inc. All rights reserved.
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            Endoplasmic Reticulum-Plasma Membrane Contact Sites.

            Yasunori Saheki, Pietro De Camilli (2017)
            The endoplasmic reticulum (ER) has a broad localization throughout the cell and forms direct physical contacts with all other classes of membranous organelles, including the plasma membrane (PM). A number of protein tethers that mediate these contacts have been identified, and study of these protein tethers has revealed a multiplicity of roles in cell physiology, including regulation of intracellular Ca2+ dynamics and signaling as well as control of lipid traffic and homeostasis. In this review, we discuss the cross talk between the ER and the PM mediated by direct contacts. We review factors that tether the two membranes, their properties, and their dynamics in response to the functional state of the cell. We focus in particular on the role of ER-PM contacts in nonvesicular lipid transport between the two bilayers mediated by lipid transfer proteins.
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              Regulation of ion channel localization and phosphorylation by neuronal activity.

              Hiroaki Misonou, Dongkai Zhen, Victor Leung … (2004)
              Voltage-dependent Kv2.1 K(+) channels, which mediate delayed rectifier Kv currents (I(K)), are expressed in large clusters on the somata and dendrites of principal pyramidal neurons, where they regulate neuronal excitability. Here we report activity-dependent changes in the localization and biophysical properties of Kv2.1. In the kainate model of continuous seizures in rat, we find a loss of Kv2.1 clustering in pyramidal neurons in vivo. Biochemical analysis of Kv2.1 in the brains of these rats shows a marked dephosphorylation of Kv2.1. In cultured rat hippocampal pyramidal neurons, glutamate stimulation rapidly causes dephosphorylation of Kv2.1, translocation of Kv2.1 from clusters to a more uniform localization, and a shift in the voltage-dependent activation of I(K). An influx of Ca(2+) leading to calcineurin activation is both necessary and sufficient for these effects. Our finding that neuronal activity modifies the phosphorylation state, localization and function of Kv2.1 suggests an important link between excitatory neurotransmission and the intrinsic excitability of pyramidal neurons.
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                Author and article information

                Contributors
                Jung-Hwa Tao-Cheng:
                ORCID: http://orcid.org/0000-0003-1897-5503
                chengs@ninds.nih.gov
                Journal
                Journal ID (nlm-ta): Mol Brain
                Journal ID (iso-abbrev): Mol Brain
                Title: Molecular Brain
                Publisher: BioMed Central (London )
                ISSN (Electronic): 1756-6606
                Publication date (Electronic): 16 April 2018
                Publication date PMC-release: 16 April 2018
                Publication date Collection: 2018
                Volume: 11
                Electronic Location Identifier: 23
                Affiliations
                ISNI 0000 0001 2177 357X, GRID grid.416870.c, NINDS Electron Microscopy Facility, National Institute of Neurological Disorders and Stroke, National Institutes of Health, ; Bethesda, MD 20892 USA
                Author information
                http://orcid.org/0000-0003-1897-5503
                Article
                Publisher ID: 366
                DOI: 10.1186/s13041-018-0366-7
                PMC ID: 5902880
                PubMed ID: 29661253
                SO-VID: fb173a75-958f-4e79-85c0-82e7ba6f3971
                Copyright © © The Author(s). 2018
                License:

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                History
                Date received : 6 March 2018
                Date accepted : 5 April 2018
                Funding
                Funded by: FundRef http://dx.doi.org/10.13039/100000065, National Institute of Neurological Disorders and Stroke;
                Award ID: intramural funds
                Categories
                Subject: Research
                Custom metadata
                issue-copyright-statement © The Author(s) 2018

                ScienceOpen disciplines: Neurosciences
                Keywords: er-pm contact sites,calcium regulation,electron microscopy
                Data availability:
                ScienceOpen disciplines: Neurosciences
                Keywords: er-pm contact sites, calcium regulation, electron microscopy

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