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      The Complex Role of Store Operated Calcium Entry Pathways and Related Proteins in the Function of Cardiac, Skeletal and Vascular Smooth Muscle Cells

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          Abstract

          Cardiac, skeletal, and smooth muscle cells shared the common feature of contraction in response to different stimuli. Agonist-induced muscle's contraction is triggered by a cytosolic free Ca 2+ concentration increase due to a rapid Ca 2+ release from intracellular stores and a transmembrane Ca 2+ influx, mainly through L-type Ca 2+ channels. Compelling evidences have demonstrated that Ca 2+ might also enter through other cationic channels such as Store-Operated Ca 2+ Channels (SOCCs), involved in several physiological functions and pathological conditions. The opening of SOCCs is regulated by the filling state of the intracellular Ca 2+ store, the sarcoplasmic reticulum, which communicates to the plasma membrane channels through the Stromal Interaction Molecule 1/2 (STIM1/2) protein. In muscle cells, SOCCs can be mainly non-selective cation channels formed by Orai1 and other members of the Transient Receptor Potential-Canonical (TRPC) channels family, as well as highly selective Ca 2+ Release-Activated Ca 2+ (CRAC) channels, formed exclusively by subunits of Orai proteins likely organized in macromolecular complexes. This review summarizes the current knowledge of the complex role of Store Operated Calcium Entry (SOCE) pathways and related proteins in the function of cardiac, skeletal, and vascular smooth muscle cells.

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          A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function.

          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.

            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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              Store-operated calcium channels.

              In electrically nonexcitable cells, Ca(2+) influx is essential for regulating a host of kinetically distinct processes involving exocytosis, enzyme control, gene regulation, cell growth and proliferation, and apoptosis. The major Ca(2+) entry pathway in these cells is the store-operated one, in which the emptying of intracellular Ca(2+) stores activates Ca(2+) influx (store-operated Ca(2+) entry, or capacitative Ca(2+) entry). Several biophysically distinct store-operated currents have been reported, but the best characterized is the Ca(2+) release-activated Ca(2+) current, I(CRAC). Although it was initially considered to function only in nonexcitable cells, growing evidence now points towards a central role for I(CRAC)-like currents in excitable cells too. In spite of intense research, the signal that relays the store Ca(2+) content to CRAC channels in the plasma membrane, as well as the molecular identity of the Ca(2+) sensor within the stores, remains elusive. Resolution of these issues would be greatly helped by the identification of the CRAC channel gene. In some systems, evidence suggests that store-operated channels might be related to TRP homologs, although no consensus has yet been reached. Better understood are mechanisms that inactivate store-operated entry and hence control the overall duration of Ca(2+) entry. Recent work has revealed a central role for mitochondria in the regulation of I(CRAC), and this is particularly prominent under physiological conditions. I(CRAC) therefore represents a dynamic interplay between endoplasmic reticulum, mitochondria, and plasma membrane. In this review, we describe the key electrophysiological features of I(CRAC) and other store-operated Ca(2+) currents and how they are regulated, and we consider recent advances that have shed insight into the molecular mechanisms involved in this ubiquitous and vital Ca(2+) entry pathway.
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                Author and article information

                Contributors
                Journal
                Front Physiol
                Front Physiol
                Front. Physiol.
                Frontiers in Physiology
                Frontiers Media S.A.
                1664-042X
                21 March 2018
                2018
                : 9
                : 257
                Affiliations
                [1] 1Department of Medical Physiology and Biophysics, University of Seville , Sevilla, Spain
                [2] 2Institute of Biomedicine of Seville, University Hospital of Virgen del Rocío, CSIC, University of Seville , Sevilla, Spain
                [3] 3CIBERCV , Madrid, Spain
                [4] 4Department of Surgery, University of Seville , Sevilla, Spain
                [5] 5Department of Stomatology, School of Dentistry, University of Seville , Sevilla, Spain
                [6] 6Cell Physiology Research Group, Department of Physiology, Institute of Molecular Pathology Biomarkers, University of Extremadura , Cáceres, Spain
                Author notes

                Edited by: Fabio Mammano, Istituto di Biologia Cellulare e Neurobiologia (CNR), Italy

                Reviewed by: John C. Chatham, University of Alabama at Birmingham, United States; Cristina Fasolato, Università degli Studi di Padova, Italy

                *Correspondence: Tarik Smani tasmani@ 123456us.es

                This article was submitted to Membrane Physiology and Membrane Biophysics, a section of the journal Frontiers in Physiology

                †These authors have contributed equally to this work.

                Article
                10.3389/fphys.2018.00257
                5872157
                29618985
                09d4091d-7377-4e02-aa48-4c51269ff0ff
                Copyright © 2018 Avila-Medina, Mayoral-Gonzalez, Dominguez-Rodriguez, Gallardo-Castillo, Ribas, Ordoñez, Rosado and Smani.

                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) and the copyright owner 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
                : 07 January 2018
                : 06 March 2018
                Page count
                Figures: 3, Tables: 0, Equations: 0, References: 175, Pages: 14, Words: 12897
                Categories
                Physiology
                Review

                Anatomy & Physiology
                ca2+,orai,stim,trpc,cardiomyocyte,skeletal muscle,vascular smooth muscle
                Anatomy & Physiology
                ca2+, orai, stim, trpc, cardiomyocyte, skeletal muscle, vascular smooth muscle

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