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      Store-Operated Ca 2+ Entry in Breast Cancer Cells: Remodeling and Functional Role

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          Abstract

          Breast cancer is the most common type of cancer in women. It is a heterogeneous disease that ranges from the less undifferentiated luminal A to the more aggressive basal or triple negative breast cancer molecular subtype. Ca 2+ influx from the extracellular medium, but more specifically store-operated Ca 2+ entry (SOCE), has been reported to play an important role in tumorigenesis and the maintenance of a variety of cancer hallmarks, including cell migration, proliferation, invasion or epithelial to mesenchymal transition. Breast cancer cells remodel the expression and functional role of the molecular components of SOCE. This review focuses on the functional role and remodeling of SOCE in breast cancer cells. The current studies suggest the need to deepen our understanding of SOCE in the biology of the different breast cancer subtypes in order to develop new and specific therapeutic strategies.

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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 539 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.
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              Orai1 is an essential pore subunit of the CRAC channel.

              Murali Prakriya, Stefan Feske, Yousang Gwack … (2006)
              Stimulation of immune cells causes depletion of Ca2+ from endoplasmic reticulum (ER) stores, thereby triggering sustained Ca2+ entry through store-operated Ca2+ release-activated Ca2+ (CRAC) channels, an essential signal for lymphocyte activation and proliferation. Recent evidence indicates that activation of CRAC current is initiated by STIM proteins, which sense ER Ca2+ levels through an EF-hand located in the ER lumen and relocalize upon store depletion into puncta closely associated with the plasma membrane. We and others recently identified Drosophila Orai and human Orai1 (also called TMEM142A) as critical components of store-operated Ca2+ entry downstream of STIM. Combined overexpression of Orai and Stim in Drosophila cells, or Orai1 and STIM1 in mammalian cells, leads to a marked increase in CRAC current. However, these experiments did not establish whether Orai is an essential intracellular link between STIM and the CRAC channel, an accessory protein in the plasma membrane, or an actual pore subunit. Here we show that Orai1 is a plasma membrane protein, and that CRAC channel function is sensitive to mutation of two conserved acidic residues in the transmembrane segments. E106D and E190Q substitutions in transmembrane helices 1 and 3, respectively, diminish Ca2+ influx, increase current carried by monovalent cations, and render the channel permeable to Cs+. These changes in ion selectivity provide strong evidence that Orai1 is a pore subunit of the CRAC channel.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: MDPI
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 14 December 2018
                Publication date Collection: December 2018
                Volume: 19
                Issue: 12
                Electronic Location Identifier: 4053
                Affiliations
                Department of Physiology, (Cellular Physiology Research Group), Institute of Molecular Pathology Biomarkers, University of Extremadura, 10003 Caceres, Spain; ijp@ 123456unex.es (I.J.); gsalido@ 123456unex.es (G.M.S.)
                Author notes
                [* ]Correspondence: jjlopez@ 123456unex.es (J.J.L.); jarosado@ 123456unex.es (J.A.R.); Tel.: +34-927251376 (J.J.L. & J.A.R.)
                Author information
                https://orcid.org/0000-0003-4575-8264
                https://orcid.org/0000-0002-5234-1478
                https://orcid.org/0000-0002-8687-2445
                https://orcid.org/0000-0002-9749-2325
                Article
                Publisher ID: ijms-19-04053
                DOI: 10.3390/ijms19124053
                PMC ID: 6321005
                PubMed ID: 30558192
                SO-VID: d1a809fe-f6f9-4f2d-a3f2-821fd945de34
                Copyright © © 2018 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 14 November 2018
                Date accepted : 11 December 2018
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: stim1,orai1,trpc channels,mcf7,mda-mb-231,calcium entry,proliferation,migration,breast cancer
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: stim1, orai1, trpc channels, mcf7, mda-mb-231, calcium entry, proliferation, migration, breast cancer

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