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      The endoplasmic reticulum: structure, function and response to cellular signaling

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          Abstract

          The endoplasmic reticulum (ER) is a large, dynamic structure that serves many roles in the cell including calcium storage, protein synthesis and lipid metabolism. The diverse functions of the ER are performed by distinct domains; consisting of tubules, sheets and the nuclear envelope. Several proteins that contribute to the overall architecture and dynamics of the ER have been identified, but many questions remain as to how the ER changes shape in response to cellular cues, cell type, cell cycle state and during development of the organism. Here we discuss what is known about the dynamics of the ER, what questions remain, and how coordinated responses add to the layers of regulation in this dynamic organelle.

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          Calcium signaling.

          David E Clapham, Md. Islam (2008)
          Calcium ions (Ca(2+)) impact nearly every aspect of cellular life. This review examines the principles of Ca(2+) signaling, from changes in protein conformations driven by Ca(2+) to the mechanisms that control Ca(2+) levels in the cytoplasm and organelles. Also discussed is the highly localized nature of Ca(2+)-mediated signal transduction and its specific roles in excitability, exocytosis, motility, apoptosis, and transcription.
          Article 0 comments Cited 1329 times – based on 0 reviews     Review now
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            A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function.

            Stefan Feske, Yousang Gwack, Murali Prakriya … (2006)
            Antigen stimulation of immune cells triggers Ca2+ entry through Ca2+ release-activated Ca2+ (CRAC) channels, promoting the immune response to pathogens by activating the transcription factor NFAT. We have previously shown that cells from patients with one form of hereditary severe combined immune deficiency (SCID) syndrome are defective in store-operated Ca2+ entry and CRAC channel function. Here we identify the genetic defect in these patients, using a combination of two unbiased genome-wide approaches: a modified linkage analysis with single-nucleotide polymorphism arrays, and a Drosophila RNA interference screen designed to identify regulators of store-operated Ca2+ entry and NFAT nuclear import. Both approaches converged on a novel protein that we call Orai1, which contains four putative transmembrane segments. The SCID patients are homozygous for a single missense mutation in ORAI1, and expression of wild-type Orai1 in SCID T cells restores store-operated Ca2+ influx and the CRAC current (I(CRAC)). We propose that Orai1 is an essential component or regulator of the CRAC channel complex.
            Article 0 comments Cited 570 times – based on 0 reviews     Review now
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              STIM1, an essential and conserved component of store-operated Ca2+ channel function

              Jack Roos, Paul J. DiGregorio, Andriy Yeromin … (2005)
              Store-operated Ca2+ (SOC) channels regulate many cellular processes, but the underlying molecular components are not well defined. Using an RNA interference (RNAi)-based screen to identify genes that alter thapsigargin (TG)-dependent Ca2+ entry, we discovered a required and conserved role of Stim in SOC influx. RNAi-mediated knockdown of Stim in Drosophila S2 cells significantly reduced TG-dependent Ca2+ entry. Patch-clamp recording revealed nearly complete suppression of the Drosophila Ca2+ release-activated Ca2+ (CRAC) current that has biophysical characteristics similar to CRAC current in human T cells. Similarly, knockdown of the human homologue STIM1 significantly reduced CRAC channel activity in Jurkat T cells. RNAi-mediated knockdown of STIM1 inhibited TG- or agonist-dependent Ca2+ entry in HEK293 or SH-SY5Y cells. Conversely, overexpression of STIM1 in HEK293 cells modestly enhanced TG-induced Ca2+ entry. We propose that STIM1, a ubiquitously expressed protein that is conserved from Drosophila to mammalian cells, plays an essential role in SOC influx and may be a common component of SOC and CRAC channels.
              Article 0 comments Cited 434 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Michael D. Blower: blower@molbio.mgh.harvard.edu
                Journal
                Journal ID (nlm-ta): Cell Mol Life Sci
                Journal ID (iso-abbrev): Cell. Mol. Life Sci
                Title: Cellular and Molecular Life Sciences
                Publisher: Springer International Publishing (Cham )
                ISSN (Print): 1420-682X
                ISSN (Electronic): 1420-9071
                Publication date (Electronic): 3 October 2015
                Publication date PMC-release: 3 October 2015
                Publication date (Print): 2016
                Volume: 73
                Pages: 79-94
                Affiliations
                [ ]Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114 USA
                [ ]Department of Genetics, Harvard Medical School, Boston, MA 02115 USA
                [ ]New England Biolabs, Ipswich, MA 01938 USA
                Article
                Publisher ID: 2052
                DOI: 10.1007/s00018-015-2052-6
                PMC ID: 4700099
                PubMed ID: 26433683
                SO-VID: 8dabb92e-05f7-4bf0-badb-11a7acb3c040
                Copyright © © The Author(s) 2015
                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.

                History
                Date received : 8 July 2015
                Date revision received : 21 September 2015
                Date accepted : 22 September 2015
                Categories
                Subject: Review
                Custom metadata
                issue-copyright-statement © Springer International Publishing 2016

                ScienceOpen disciplines: Molecular biology
                Keywords: interphase,mitosis,unfolded protein response,organization,fertilization,phosphorylation
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: interphase, mitosis, unfolded protein response, organization, fertilization, phosphorylation

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