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Dependent Activation
Ca2؉-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2؉-dependent activation Shumin Bian*, Isabelle Favre*†, and Edward Moczydlowski*‡§ Departments of *Pharmacology and ‡Cellular and Molecular Physiology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520-8066 Communicated by Ramon Latorre, Center for Scientific Studies of Santiago, Valdivia, Chile, February 13, 2001 (received for review November 28, 2000) Mutational and biophysical analysis suggests that an intracellular S0–S6 plus a portion of the COOH terminus, whereas the Ϸ400 .(COOH-terminal domain of the large conductance Ca2؉-activated residue sequence following the linker comprises the Tail (Fig. 1 K؉ channel (BK channel) contains Ca2؉-binding site(s) that are Experiments with chimeric Core-Tail constructs by using Slo1 allosterically coupled to channel opening. However the structural genes of different species suggest that the Ca2ϩ-sensing function basis of Ca2؉ binding to BK channels is unknown. To pursue this of the channel is associated with the Tail domain (9). More question, we overexpressed the COOH-terminal 280 residues of the recent studies making use of the Ca2ϩ-insensitive Slo3 Kϩ Drosophila slowpoke BK channel (Dslo-C280) as a FLAG- and His6- channel gene verified that specific regions of protein sequence tagged protein in Escherichia coli. We purified Dslo-C280 in soluble within the Tail confer the property of Ca2ϩ-dependent gating ؉ ؉ form and used a 45Ca2 -overlay protein blot assay to detect Ca2 (10). Complementary mutational studies identified an Asp-rich ؉ binding. Dslo-C280 exhibits specific binding of 45Ca2 in compari- sequence motif in the Tail domain (Fig. -
Bryostatin Enhancement of Memory in Hermissenda
Reference: Biol. Bull. 210: 201–214. (June 2006) A contribution to The Biological Bulletin Virtual Symposium © 2006 Marine Biological Laboratory on Marine Invertebrate Models of Learning and Memory. Bryostatin Enhancement of Memory in Hermissenda A. M. KUZIRIAN1,*, H. T. EPSTEIN1, C. J. GAGLIARDI1,2, T. J. NELSON3, M. SAKAKIBARA4, C. TAYLOR5, A. B. SCIOLETTI1,6, AND D. L. ALKON3 1 Marine Biological Laboratory, Woods Hole, Massachusetts 02543; 2 Science Department, Roger Williams University, Bristol, Rhode Island 02809; 3 Blanchette Rockefeller Neurosciences Institute, Johns Hopkins University, Rockville, Maryland 20850; 4 Department of Biological Science and Technology, Tokai University, Shizuoka, Japan; 5 Department of Biology, University of Michigan, Ann Arbor, Michigan 48104; and 6 Northeastern University, Boston, Massachusetts 02115 Abstract. Bryostatin, a potent agonist of protein kinase C bryostatin revealed changes in input resistance and an en- (PKC), when administered to Hermissenda was found to hanced long-lasting depolarization (LLD) in response to affect acquisition of an associative learning paradigm. Low light. Likewise, quantitative immunocytochemical measure- bryostatin concentrations (0.1 to 0.5 ng/ml) enhanced mem- ments using an antibody specific for the PKC-activated ϩ ory acquisition, while concentrations higher than 1.0 ng/ml Ca2 /GTP-binding protein calexcitin showed enhanced an- down-regulated the pathway and no recall of the associative tibody labeling with bryostatin. training was exhibited. The extent of enhancement de- Animals exposed to the PKC inhibitor bisindolylmaleim- pended upon the conditioning regime used and the memory ide-XI (Ro-32-0432) administered by immersion prior to stage normally fostered by that regime. The effects of two 9-TE conditioning showed no training-induced changes training events (TEs) with paired conditioned and uncondi- with or without bryostatin exposure. -
Minding the Calcium Store: Ryanodine Receptor Activation As a Convergent Mechanism of PCB Toxicity
Pharmacology & Therapeutics 125 (2010) 260–285 Contents lists available at ScienceDirect Pharmacology & Therapeutics journal homepage: www.elsevier.com/locate/pharmthera Associate Editor: Carey Pope Minding the calcium store: Ryanodine receptor activation as a convergent mechanism of PCB toxicity Isaac N. Pessah ⁎, Gennady Cherednichenko, Pamela J. Lein Department of Molecular Biosciences, School of Veterinary Medicine, University of California, Davis, CA 95616, USA article info abstract Keywords: Chronic low-level polychlorinated biphenyl (PCB) exposures remain a significant public health concern since Ryanodine receptor (RyR) results from epidemiological studies indicate that PCB burden is associated with immune system Calcium-induced calcium release dysfunction, cardiovascular disease, and impairment of the developing nervous system. Of these various Calcium regulation adverse health effects, developmental neurotoxicity has emerged as a particularly vulnerable endpoint in Polychlorinated biphenyls PCB toxicity. Arguably the most pervasive biological effects of PCBs could be mediated by their ability to alter Triclosan fi 2+ Bastadins the spatial and temporal delity of Ca signals through one or more receptor-mediated processes. This Polybrominated diphenylethers review will focus on our current knowledge of the structure and function of ryanodine receptors (RyRs) in Developmental neurotoxicity muscle and nerve cells and how PCBs and related non-coplanar structures alter these functions. The Activity dependent plasticity molecular and cellular mechanisms by which non-coplanar PCBs and related structures alter local and global Ca2+ signaling properties and the possible short and long-term consequences of these perturbations on neurodevelopment and neurodegeneration are reviewed. © 2009 Elsevier Inc. All rights reserved. Contents 1. Introduction ............................................... 260 2. Ryanodine receptor macromolecular complexes: significance to polychlorinated biphenyl-mediated Ca2+ dysregulation . -
Neuronal Calcium Sensor-1 Modulation of Optimal Calcium Level for Neurite Outgrowth Kwokyin Hui1, Guang-He Fei1, Bechara J
RESEARCH ARTICLE 4479 Development 134, 4479-4489 (2007) doi:10.1242/dev.008979 Neuronal calcium sensor-1 modulation of optimal calcium level for neurite outgrowth Kwokyin Hui1, Guang-He Fei1, Bechara J. Saab2,3, Jiang Su1, John C. Roder2,3 and Zhong-Ping Feng1,* Neurite extension and branching are affected by activity-dependent modulation of intracellular Ca2+, such that an optimal window 2+ 2+ of [Ca ]i is required for outgrowth. Our understanding of the molecular mechanisms regulating this optimal [Ca ]i remains unclear. Taking advantage of the large growth cone size of cultured primary neurons from pond snail Lymnaea stagnalis combined with dsRNA knockdown, we show that neuronal calcium sensor-1 (NCS-1) regulates neurite extension and branching, and activity- dependent Ca2+ signals in growth cones. An NCS-1 C-terminal peptide enhances only neurite branching and moderately reduces the Ca2+ signal in growth cones compared with dsRNA knockdown. Our findings suggest that at least two separate structural domains in NCS-1 independently regulate Ca2+ influx and neurite outgrowth, with the C-terminus specifically affecting branching. We describe a model in which NCS-1 regulates cytosolic Ca2+ around the optimal window level to differentially control neurite extension and branching. KEY WORDS: NCS-1, Neurite outgrowth, Activity-dependent calcium signals, fura-2 imaging, Lymnaea stagnalis INTRODUCTION There is compelling evidence that NCS-1 is involved in neurite Neurite extension and branching are affected by activity-dependent development in a few systems. For instance, NCS-1 expression modulation of intracellular Ca2+ (Komuro and Rakic, 1996; Tang et increases in grey matter and decreases in white matter during 2+ al., 2003; Zheng, 2000), such that an optimal window of [Ca ]i is embryogenesis and early postnatal stages (Kawasaki et al., 2003). -
Modulation of Neuronal Ryanodine Receptor-Mediated Calcium
MODULATION OF NEURONAL RYANODINE RECEPTOR-MEDIATED CALCIUM SIGNALING BY CALSENILIN A DISSERTATION IN Cell Biology and Biophysics and Molecular Biology and Biochemistry Presented to the Faculty of the University of Missouri-Kansas City in partial fulfillment of the requirements for the degree DOCTOR OF PHILOSOPHY by MICHAEL ANTHONY GRILLO M.S., University of Missouri-Kansas City, Kansas City, MO 2010 B.S., Texas Wesleyan University, TX, 2000 Kansas City, MO 2013 2013 MICHAEL ANTHONY GRILLO ALL RIGHTS RESERVED MODULATION OF NEURONAL RYANODINE RECEPTOR-MEDIATED CALCIUM SIGNALING BY CALSENILIN Michael Anthony Grillo, Candidate for the Doctor of Philosophy Degree University of Missouri-Kansas City, 2013 ABSTRACT Calsenilin is calcium (Ca2+) ion Ca2+ binding protein found in the nucleus, plasma membrane, and endoplasmic reticulum of neuronal cells. Calsenilin was first found to interact with two proteins involved in early-onset familial Alzheimer disease (AD), presenilin 1 and presenilin 2. Several studies have shown overexpression of calsenilin to alter Ca2+ signaling and cell viability in several neuronal cell models of AD. In this study, we show that calsenilin directly interacts with the ryanodine receptor (RyR) modulating Ca2+ release from this intracellular Ca2+-activated Ca2+ release channel. Co-expression, co-localization, and protein-protein interaction of calsenilin and RyR in primary neurons and in central nervous system tissue were determined using immunoblotting, immunohistochemistry and co-immunoprecipitation. Mechanisms of intracellular Ca2+- signaling controlled by the interaction of calsenilin and RyR, including changes in the release of Ca2+ from intracellular stores, were measured with single channel electrophysiology and live-cell optical imaging techniques. Immunohistochemical studies showed a high degree of co-localization between calsenilin and the RyR in neurons of the central nervous system. -
A FAMILY of NEURONAL Ca2+-BINDING PROTEINS WITH
Neuroscience Vol. 112, No. 1, pp. 51^63, 2002 ß 2002 IBRO. Published by Elsevier Science Ltd All rights reserved. Printed in Great Britain PII: S0306-4522(02)00063-5 0306-4522 / 02 $22.00+0.00 www.neuroscience-ibro.com NECABS: A FAMILY OF NEURONAL Ca2þ-BINDING PROTEINS WITH AN UNUSUAL DOMAIN STRUCTURE AND A RESTRICTED EXPRESSION PATTERN S. SUGITA,1 A. HO and T. C. SUº DHOFÃ Center for Basic Neuroscience, Department of Molecular Genetics, and Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75235, USA AbstractöCa2þ-signalling plays a major role in regulating all aspects of neuronal function. Di¡erent types of neurons exhibit characteristic di¡erences in the responses to Ca2þ-signals. Correlating with di¡erences in Ca2þ-response are expression patterns of Ca2þ-binding proteins that often serve as markers for various types of neurons. For example, in the cerebral cortex the EF-hand Ca2þ-binding proteins parvalbumin and calbindin are primarily expressed in inhibitory interneurons where they in£uence Ca2þ-dependent responses. We have now identi¢ed a new family of proteins called NECABs (neuronal Ca2þ-binding proteins). NECABs contain an N-terminal EF-hand domain that binds Ca2þ, but di¡erent from many other neuronal EF-hand Ca2þ-binding proteins, only a single EF-hand domain is present. At the C-terminus, NECABs include a DUF176 motif, a bacterial domain of unknown function that was previously not observed in eukaryotes. In rat at least three closely related NECAB genes are expressed either primarily in brain (NECABs 1 and 2) or in brain and muscle (NECAB 3). -
Molecular Dynamics of the Neuronal Ca -Binding Proteins
Molecular dynamics of the neuronal Ca2+ -binding proteins Caldendrin and Calneurons Dissertation zur Erlangung des akademischen Grades doctor rerum naturalium (Dr. rer. nat.) genehmigt durch die Fakultät für Naturwissenschaften der Otto-von-Guericke-Universität Magdeburg von Diplom-Biologin Marina Gennadievna Mikhaylova geb. am 1 März 1981 in Ufa, Russland Gutachter: Prof. Dr. E.D. Gundelfinger am: 30.07.2009 vorgelegt von: Diplom-Biologin Marina Gennadievna Mikhaylova Acknowledgements This thesis is the account of almost four years of devoted work at the Leibniz Institute for Neurobiology Magdeburg in the group of Michael R. Kreutz (Project Group Neuroplasticity) which would not have been possible without the help of many friends and colleagues. First of all, I would like to thank Michael for being a great advisor. His ideas and tremendous support had a major influence on this thesis. I want to thank Anna Karpova for being my friend and colleague for many years. I enjoyed to do research together with her as well as the nice discussions we daily had. Many thanks also to Prof. Eckart D Gundelfinger for his encouraging discussions and help with corrections of the papers. My thanks to Thomas Munsch, Peter Landgraf, Karl-Heinz Smalla, Ulrich Thomas, Oliver Kobler, Yogendra Sharma and Thomas Behnisch for the great collaboration over the years. It was a pleasure to work with all these people and to benefit from their knowledge. My thanks to Paramesh Pasham Reddy, Anne-Christin Lehman, Johannes Hradsky and Philipp Bethge for their collaboration, support and friendship while doing their Ph.D studies, diploma theses or internships in our group. -
The Calcium Sensor Synaptotagmin 7 Is Required for Synaptic Facilitation
The calcium sensor synaptotagmin 7 is required for synaptic facilitation The Harvard community has made this article openly available. Please share how this access benefits you. Your story matters Citation Jackman, Skyler L., Josef Turecek, Justine E. Belinsky, and Wade G. Regehr. 2015. “The calcium sensor synaptotagmin 7 is required for synaptic facilitation.” Nature 529 (7584): 88-91. doi:10.1038/ nature16507. http://dx.doi.org/10.1038/nature16507. Published Version doi:10.1038/nature16507 Citable link http://nrs.harvard.edu/urn-3:HUL.InstRepos:27822294 Terms of Use This article was downloaded from Harvard University’s DASH repository, and is made available under the terms and conditions applicable to Other Posted Material, as set forth at http:// nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of- use#LAA HHS Public Access Author manuscript Author Manuscript Author ManuscriptNature. Author ManuscriptAuthor manuscript; Author Manuscript available in PMC 2016 July 07. Published in final edited form as: Nature. 2016 January 7; 529(7584): 88–91. doi:10.1038/nature16507. The calcium sensor synaptotagmin 7 is required for synaptic facilitation Skyler L. Jackman1, Josef Turecek1, Justine E. Belinsky1, and Wade G. Regehr1 1Department of Neurobiology, Harvard Medical School, 220 Longwood Avenue, Boston, Massachusetts 02115, USA Abstract It has been known for over 70 years that synaptic strength is dynamically regulated in a use- dependent manner1. At synapses with a low initial release probability, closely spaced presynaptic action potentials can result in facilitation, a short-term form of enhancement where each subsequent action potential evokes greater neurotransmitter release2. Facilitation can enhance neurotransmitter release manyfold and profoundly influence information transfer across synapses3, but the underlying mechanism remains a mystery. -
The Genie in the Bottle-Magnified Calcium Signaling in Dorsolateral
Molecular Psychiatry https://doi.org/10.1038/s41380-020-00973-3 EXPERT REVIEW The genie in the bottle-magnified calcium signaling in dorsolateral prefrontal cortex 1 1 1 Amy F. T. Arnsten ● Dibyadeep Datta ● Min Wang Received: 27 August 2020 / Revised: 20 November 2020 / Accepted: 26 November 2020 © The Author(s) 2020. This article is published with open access Abstract Neurons in the association cortices are particularly vulnerable in cognitive disorders such as schizophrenia and Alzheimer’s disease, while those in primary visual cortex remain relatively resilient. This review proposes that the special molecular mechanisms needed for higher cognitive operations confer vulnerability to dysfunction, atrophy, and neurodegeneration when regulation is lost due to genetic and/or environmental insults. Accumulating data suggest that higher cortical circuits rely on magnified levels of calcium (from NMDAR, calcium channels, and/or internal release from the smooth endoplasmic reticulum) near the postsynaptic density to promote the persistent firing needed to maintain, manipulate, and store information without “bottom-up” sensory stimulation. For example, dendritic spines in the primate dorsolateral prefrontal – – 1234567890();,: 1234567890();,: cortex (dlPFC) express the molecular machinery for feedforward, cAMP PKA calcium signaling. PKA can drive internal calcium release and promote calcium flow through NMDAR and calcium channels, while in turn, calcium activates adenylyl cyclases to produce more cAMP–PKA signaling. Excessive levels of cAMP–calcium signaling can have a number of detrimental effects: for example, opening nearby K+ channels to weaken synaptic efficacy and reduce neuronal firing, and over a longer timeframe, driving calcium overload of mitochondria to induce inflammation and dendritic atrophy. Thus, calcium–cAMP signaling must be tightly regulated, e.g., by agents that catabolize cAMP or inhibit its production (PDE4, mGluR3), and by proteins that bind calcium in the cytosol (calbindin). -
New Approach for Untangling the Role of Uncommon Calcium-Binding Proteins in the Central Nervous System
brain sciences Review New Approach for Untangling the Role of Uncommon Calcium-Binding Proteins in the Central Nervous System Krisztina Kelemen * and Tibor Szilágyi Department of Physiology, Doctoral School, Faculty of Medicine, George Emil Palade University of Medicine, Pharmacy, Science, and Technology of Targu Mures, 540142 Târgu Mures, , Romania; [email protected] * Correspondence: [email protected]; Tel.: +40-746-248064 Abstract: Although Ca2+ ion plays an essential role in cellular physiology, calcium-binding proteins (CaBPs) were long used for mainly as immunohistochemical markers of specific cell types in different regions of the central nervous system. They are a heterogeneous and wide-ranging group of proteins. Their function was studied intensively in the last two decades and a tremendous amount of informa- tion was gathered about them. Girard et al. compiled a comprehensive list of the gene-expression profiles of the entire EF-hand gene superfamily in the murine brain. We selected from this database those CaBPs which are related to information processing and/or neuronal signalling, have a Ca2+- buffer activity, Ca2+-sensor activity, modulator of Ca2+-channel activity, or a yet unknown function. In this way we created a gene function-based selection of the CaBPs. We cross-referenced these findings with publicly available, high-quality RNA-sequencing and in situ hybridization databases (Human Protein Atlas (HPA), Brain RNA-seq database and Allen Brain Atlas integrated into the HPA) and created gene expression heat maps of the regional and cell type-specific expression levels of the selected CaBPs. This represents a useful tool to predict and investigate different expression patterns and functions of the less-known CaBPs of the central nervous system. -
Neuronal Calcium Sensor-1 Enhancement of Insp3 Receptor Activity Is Inhibited by Therapeutic Levels of Lithium
Neuronal calcium sensor-1 enhancement of InsP3 receptor activity is inhibited by therapeutic levels of lithium Christina Schlecker, … , Klara Szigeti-Buck, Barbara E. Ehrlich J Clin Invest. 2006;116(6):1668-1674. https://doi.org/10.1172/JCI22466. Research Article Neuroscience Regulation and dysregulation of intracellular calcium (Ca2+) signaling via the inositol 1,4,5-trisphosphate receptor (InsP3R) has been linked to many cellular processes and pathological conditions. In the present study, addition of neuronal calcium sensor-1 (NCS-1), a high-affinity, low-capacity, calcium-binding protein, to purified InsP3R type 1 (InsP3R1) increased the channel activity in both a calcium-dependent and -independent manner. In intact cells, enhanced expression of NCS-1 resulted in increased intracellular calcium release upon stimulation of the phosphoinositide signaling pathway. To determine whether InsP3R1/NCS-1 interaction could be functionally relevant in bipolar disorders, conditions in which NCS-1 is highly expressed, we tested the effect of lithium, a salt widely used for treatment of bipolar disorders. Lithium inhibited the enhancing effect of NCS-1 on InsP3R1 function, suggesting that InsP3R1/NCS-1 interaction is an essential component of the pathomechanism of bipolar disorder. Find the latest version: https://jci.me/22466/pdf Research article Neuronal calcium sensor-1 enhancement of InsP3 receptor activity is inhibited by therapeutic levels of lithium Christina Schlecker,1,2,3 Wolfgang Boehmerle,1,4 Andreas Jeromin,5 Brenda DeGray,1 Anurag Varshney,1 Yogendra Sharma,6 Klara Szigeti-Buck,7 and Barbara E. Ehrlich1,3 1Department of Pharmacology, Yale University, New Haven, Connecticut, USA. 2Department of Neuroscience, University of Magdeburg, Magdeburg, Germany. -
Crystallization and Preliminary X-Ray Diffraction Analysis of Calexcitin From
crystallization communications Acta Crystallographica Section F Structural Biology Crystallization and preliminary X-ray diffraction and Crystallization analysis of calexcitin from Loligo pealei: a neuronal Communications protein implicated in learning and memory ISSN 1744-3091 G. D. E. Beaven,a P. T. Erskine,a The neuronal protein calexcitin from the long-finned squid Loligo pealei has J. N. Wright,a F. Mohammed,a‡ been expressed in Escherichia coli and purified to homogeneity. Calexcitin is a R. Gill,a S. P. Wood,a J. Vernon,b 22 kDa calcium-binding protein that becomes up-regulated in invertebrates K. P. Gieseb and J. B. Coopera* following Pavlovian conditioning and is likely to be involved in signal transduction events associated with learning and memory. Recombinant squid aSchool of Biological Sciences, University of calexcitin has been crystallized using the hanging-drop vapour-diffusion Southampton, Bassett Crescent East, technique in the orthorhombic space group P212121. The unit-cell parameters Southampton SO16 7PX, England, and of a = 46.6, b = 69.2, c = 134.8 A˚ suggest that the crystals contain two monomers bWolfson Institute for Biomedical Research, per asymmetric unit and have a solvent content of 49%. This crystal form University College London, Cruciform Building, diffracts X-rays to at least 1.8 A˚ resolution and yields data of high quality using Gower Street, London WC1E 6BT, England synchrotron radiation. ‡ Present address: CRUK Institute for Cancer Studies, University of Birmingham, Vincent 1. Introduction Drive, Edgbaston, Birmingham B15 2TT, England. The protein calexcitin was originally identified in the photoreceptor neurons of the marine snail Hermissenda crassicornis as a 20 kDa protein that became up-regulated and phosphorylated following a Correspondence e-mail: Pavlovian training protocol (Nelson et al., 1990).