Inviting an author to review:
Find an author and click ‘Invite to review selected article’ near their name.
Search for authorsSearch for similar articles
193
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      EF hand-mediated Ca 2+- and cGMP-signaling in photoreceptor synaptic terminals

      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

          Photoreceptors, the light-sensitive receptor neurons of the retina, receive and transmit a plethora of visual informations from the surrounding world. Photoreceptors capture light and convert this energy into electrical signals that are conveyed to the inner retina. For synaptic communication with the inner retina, photoreceptors make large active zones that are marked by synaptic ribbons. These unique synapses support continuous vesicle exocytosis that is modulated by light-induced, graded changes of membrane potential. Synaptic transmission can be adjusted in an activity-dependent manner, and at the synaptic ribbons, Ca 2+- and cGMP-dependent processes appear to play a central role. EF-hand-containing proteins mediate many of these Ca 2+- and cGMP-dependent functions. Since continuous signaling of photoreceptors appears to be prone to malfunction, disturbances of Ca 2+- and cGMP-mediated signaling in photoreceptors can lead to visual defects, retinal degeneration (rd), and even blindness. This review summarizes aspects of signal transmission at the photoreceptor presynaptic terminals that involve EF-hand-containing Ca 2+-binding proteins.

          Related collections

          Most cited references131

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

          Voltage-gated calcium channels.

          Voltage-gated calcium (Ca(2+)) channels are key transducers of membrane potential changes into intracellular Ca(2+) transients that initiate many physiological events. There are ten members of the voltage-gated Ca(2+) channel family in mammals, and they serve distinct roles in cellular signal transduction. The Ca(V)1 subfamily initiates contraction, secretion, regulation of gene expression, integration of synaptic input in neurons, and synaptic transmission at ribbon synapses in specialized sensory cells. The Ca(V)2 subfamily is primarily responsible for initiation of synaptic transmission at fast synapses. The Ca(V)3 subfamily is important for repetitive firing of action potentials in rhythmically firing cells such as cardiac myocytes and thalamic neurons. This article presents the molecular relationships and physiological functions of these Ca(2+) channel proteins and provides information on their molecular, genetic, physiological, and pharmacological properties.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Multiple roles of calcium ions in the regulation of neurotransmitter release.

            The intracellular calcium concentration ([Ca(2+)]) has important roles in the triggering of neurotransmitter release and the regulation of short-term plasticity (STP). Transmitter release is initiated by quite high concentrations within microdomains, while short-term facilitation is strongly influenced by the global buildup of "residual calcium." A global rise in [Ca(2+)] also accelerates the recruitment of release-ready vesicles, thereby controlling the degree of short-term depression (STD) during sustained activity, as well as the recovery of the vesicle pool in periods of rest. We survey data that lead us to propose two distinct roles of [Ca(2+)] in vesicle recruitment: one accelerating "molecular priming" (vesicle docking and the buildup of a release machinery), the other promoting the tight coupling between releasable vesicles and Ca(2+) channels. Such coupling is essential for rendering vesicles sensitive to short [Ca(2+)] transients, generated during action potentials.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              RIM proteins tether Ca2+ channels to presynaptic active zones via a direct PDZ-domain interaction.

              At a synapse, fast synchronous neurotransmitter release requires localization of Ca(2+) channels to presynaptic active zones. How Ca(2+) channels are recruited to active zones, however, remains unknown. Using unbiased yeast two-hybrid screens, we here identify a direct interaction of the central PDZ domain of the active-zone protein RIM with the C termini of presynaptic N- and P/Q-type Ca(2+) channels but not L-type Ca(2+) channels. To test the physiological significance of this interaction, we generated conditional knockout mice lacking all multidomain RIM isoforms. Deletion of RIM proteins ablated most neurotransmitter release by simultaneously impairing the priming of synaptic vesicles and by decreasing the presynaptic localization of Ca(2+) channels. Strikingly, rescue of the decreased Ca(2+)-channel localization required the RIM PDZ domain, whereas rescue of vesicle priming required the RIM N terminus. We propose that RIMs tether N- and P/Q-type Ca(2+) channels to presynaptic active zones via a direct PDZ-domain-mediated interaction, thereby enabling fast, synchronous triggering of neurotransmitter release at a synapse. Copyright © 2011 Elsevier Inc. All rights reserved.
                Bookmark

                Author and article information

                Journal
                Front Mol Neurosci
                Front. Mol. Neurosci.
                Frontiers in Molecular Neuroscience
                Frontiers Media S.A.
                1662-5099
                25 January 2012
                29 February 2012
                2012
                : 5
                : 26
                Affiliations
                simpleDepartment of Neuroanatomy, Medical School Homburg/Saar, Institute for Anatomy and Cell Biology, Saarland University Saarland, Germany
                Author notes

                Edited by: Karl-Wilhelm Koch, Carl von Ossietzky University Oldenburg, Germany

                Reviewed by: Karl-Wilhelm Koch, Carl von Ossietzky University Oldenburg, Germany; Florentina Soto, Washington University in St. Louis, USA

                *Correspondence: Frank Schmitz and Chad P. Grabner, Department of Neuroanatomy, Medical School Homburg/Saar, Institute for Anatomy and Cell Biology, Saarland University, Kirrbergerstrasse, University Campus, 66421 Homburg/Saar, Germany. e-mail: frank.schmitz@ 123456uks.eu ; chadgrabner@ 123456gmail.com

                †Present Address: Department of Experimental Orthopedics, Saarland University, University Hospital of Orthopedics, Homburg/Saar, Germany.

                Article
                10.3389/fnmol.2012.00026
                3289946
                22393316
                8646de4d-6e4c-4b4a-8cb8-ea9b1cbc581f
                Copyright © 2012 Schmitz, Natarajan, Venkatesan, Wahl, Schwarz and Grabner.

                This is an open-access article distributed under the terms of the Creative Commons Attribution Non Commercial License, which permits non-commercial use, distribution, and reproduction in other forums, provided the original authors and source are credited.

                History
                : 09 January 2012
                : 15 February 2012
                Page count
                Figures: 5, Tables: 0, Equations: 0, References: 148, Pages: 15, Words: 12945
                Categories
                Neuroscience
                Review Article

                Neurosciences
                ribbon synapse,ef-hands,synaptic ribbon,cabp4,ribeye,gcap,photoreceptor,cav1.4 calcium channel
                Neurosciences
                ribbon synapse, ef-hands, synaptic ribbon, cabp4, ribeye, gcap, photoreceptor, cav1.4 calcium channel

                Comments

                Comment on this article