20
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      A focus on extracellular Ca 2+ entry into skeletal muscle

      review-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The main task of skeletal muscle is contraction and relaxation for body movement and posture maintenance. During contraction and relaxation, Ca 2+ in the cytosol has a critical role in activating and deactivating a series of contractile proteins. In skeletal muscle, the cytosolic Ca 2+ level is mainly determined by Ca 2+ movements between the cytosol and the sarcoplasmic reticulum. The importance of Ca 2+ entry from extracellular spaces to the cytosol has gained significant attention over the past decade. Store-operated Ca 2+ entry with a low amplitude and relatively slow kinetics is a main extracellular Ca 2+ entryway into skeletal muscle. Herein, recent studies on extracellular Ca 2+ entry into skeletal muscle are reviewed along with descriptions of the proteins that are related to extracellular Ca 2+ entry and their influences on skeletal muscle function and disease.

          Related collections

          Most cited references162

          • Record: found
          • Abstract: found
          • Article: not found

          TRP channels as cellular sensors.

          TRP channels are the vanguard of our sensory systems, responding to temperature, touch, pain, osmolarity, pheromones, taste and other stimuli. But their role is much broader than classical sensory transduction. They are an ancient sensory apparatus for the cell, not just the multicellular organism, and they have been adapted to respond to all manner of stimuli, from both within and outside the cell.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            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.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              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.
                Bookmark

                Author and article information

                Journal
                Exp Mol Med
                Exp. Mol. Med
                Experimental & Molecular Medicine
                Nature Publishing Group
                1226-3613
                2092-6413
                September 2017
                15 September 2017
                1 September 2017
                : 49
                : 9
                : e378
                Affiliations
                [1 ]Department of Pharmacology, College of Medicine, Seoul National University , Seoul, Republic of Korea
                [2 ]Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles , Los Angeles, CA, USA
                [3 ]Department of Anesthesia, Perioperative and Pain Medicine, Brigham and Women’s Hospital, Harvard Medical School , Boston, MA, USA
                [4 ]Department of Physiology, College of Medicine, The Catholic University of Korea , Seoul, Republic of Korea
                Author notes
                [* ]Department of Physiology, College of Medicine, The Catholic University of Korea , 222 Banpo-daero, Seocho-gu, Seoul 06591, Republic of Korea. E-mail: ehui@ 123456catholic.ac.kr
                Article
                emm2017208
                10.1038/emm.2017.208
                5628281
                28912570
                4341599e-199d-46eb-b776-74a03029685e
                Copyright © 2017 The Author(s)

                This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/

                History
                : 18 April 2017
                : 16 June 2017
                : 28 June 2017
                Categories
                Review

                Molecular medicine
                Molecular medicine

                Comments

                Comment on this article