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      Emerging Roles of L-Type Voltage-Gated and Other Calcium Channels in T Lymphocytes

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          Abstract

          In T lymphocytes, calcium ion controls a variety of biological processes including development, survival, proliferation, and effector functions. These distinct and specific roles are regulated by different calcium signals, which are generated by various plasma membrane calcium channels. The repertoire of calcium-conducting proteins in T lymphocytes includes store-operated CRAC channels, transient receptor potential channels, P2X channels, and L-type voltage-gated calcium (Ca v1) channels. In this paper, we will focus mainly on the role of the Ca v1 channels found expressed by T lymphocytes, where these channels appear to operate in a T cell receptor stimulation-dependent and voltage sensor independent manner. We will review their expression profile at various differentiation stages of CD4 and CD8 T lymphocytes. Then, we will present crucial genetic evidence in favor of a role of these Ca v1 channels and related regulatory proteins in both CD4 and CD8 T cell functions such as proliferation, survival, cytokine production, and cytolysis. Finally, we will provide evidence and speculate on how these voltage-gated channels might function in the T lymphocyte, a non-excitable cell.

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          TRP channels.

          Kartik Venkatachalam, Craig Montell (2007)
          The TRP (Transient Receptor Potential) superfamily of cation channels is remarkable in that it displays greater diversity in activation mechanisms and selectivities than any other group of ion channels. The domain organizations of some TRP proteins are also unusual, as they consist of linked channel and enzyme domains. A unifying theme in this group is that TRP proteins play critical roles in sensory physiology, which include contributions to vision, taste, olfaction, hearing, touch, and thermo- and osmosensation. In addition, TRP channels enable individual cells to sense changes in their local environment. Many TRP channels are activated by a variety of different stimuli and function as signal integrators. The TRP superfamily is divided into seven subfamilies: the five group 1 TRPs (TRPC, TRPV, TRPM, TRPN, and TRPA) and two group 2 subfamilies (TRPP and TRPML). TRP channels are important for human health as mutations in at least four TRP channels underlie disease.
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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.
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              STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx.

              Jen Liou, Man Lyang Kim, Won Do Heo … (2005)
              Ca(2+) signaling in nonexcitable cells is typically initiated by receptor-triggered production of inositol-1,4,5-trisphosphate and the release of Ca(2+) from intracellular stores. An elusive signaling process senses the Ca(2+) store depletion and triggers the opening of plasma membrane Ca(2+) channels. The resulting sustained Ca(2+) signals are required for many physiological responses, such as T cell activation and differentiation. Here, we monitored receptor-triggered Ca(2+) signals in cells transfected with siRNAs against 2,304 human signaling proteins, and we identified two proteins required for Ca(2+)-store-depletion-mediated Ca(2+) influx, STIM1 and STIM2. These proteins have a single transmembrane region with a putative Ca(2+) binding domain in the lumen of the endoplasmic reticulum. Ca(2+) store depletion led to a rapid translocation of STIM1 into puncta that accumulated near the plasma membrane. Introducing a point mutation in the STIM1 Ca(2+) binding domain resulted in prelocalization of the protein in puncta, and this mutant failed to respond to store depletion. Our study suggests that STIM proteins function as Ca(2+) store sensors in the signaling pathway connecting Ca(2+) store depletion to Ca(2+) influx.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Front Immunol
                Journal ID (iso-abbrev): Front Immunol
                Journal ID (publisher-id): Front. Immunol.
                Title: Frontiers in Immunology
                Publisher: Frontiers Media S.A.
                ISSN (Electronic): 1664-3224
                Publication date (Electronic): 30 August 2013
                Publication date Collection: 2013
                Volume: 4
                Electronic Location Identifier: 243
                Affiliations
                [1] 1Equipe de recherche Environnement et Santé, Faculté Polydisciplinaire de Safi, Université Cadi Ayyad , Safi, Morocco
                [2] 2Trudeau Institute , Saranac Lake, NY, USA
                [3] 3Department of Cardiothoracic Surgery, Hadassah Medical Center , Jerusalem, Israel
                [4] 4Flavell Laboratory, Department of Immunobiology, Yale University School of Medicine , New Haven, CT, USA
                [5] 5Howard Hughes Medical Institute , New Haven, CT, USA
                Author notes

                Edited by: Gergely Toldi, Semmelweis University, Hungary

                Reviewed by: Christian Schönbach, Kyushu Institute of Technology, Japan; Tomasz Zal, University of Texas MD Anderson Cancer Center, USA

                *Correspondence: Richard A. Flavell, Yale University School of Medicine, 300 Cedar Street, TAC S-569, New Haven, CT 06520-8011, USA e-mail: richard.flavell@ 123456yale.edu

                †Abdallah Badou and Mithilesh K. Jha have contributed equally to this work.

                This article was submitted to T Cell Biology, a section of the journal Frontiers in Immunology.

                Article
                DOI: 10.3389/fimmu.2013.00243
                PMC ID: 3757574
                PubMed ID: 24009608
                SO-VID: 935aa293-52f6-4b8f-97b4-6a1bc3db2ab5
                Copyright © Copyright © 2013 Badou, Jha, Matza and Flavell.
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                Date received : 31 May 2013
                Date accepted : 05 August 2013
                Page count
                Figures: 1, Tables: 1, Equations: 0, References: 95, Pages: 10, Words: 9644
                Categories
                Subject: Immunology
                Subject: Review Article

                ScienceOpen disciplines: Immunology
                Keywords: cav1 channels,calcium channels,cd4 t cells,cd8 t cells,crac channel
                Data availability:
                ScienceOpen disciplines: Immunology
                Keywords: cav1 channels, calcium channels, cd4 t cells, cd8 t cells, crac channel

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