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1. Storm impacts on phytoplankton community dynamics in lakes

Author

Vijay P. Patil, Wim Thiery, Emily R. Nodine, Stephen J. Thackeray, Aleksandra M. Lewandowska, Alfred Theodore Nutefe Kwasi Kpodonu, Francesco Pomati, Maria Eugenia del Rosario Llames, Ruchi Bhattacharya, Tanner J. Williamson, Orlane Anneville, Patrick Venail, Cayelan C. Carey, Nico Salmaso, Marc J. Lajeunesse, Harriet L. Wilson, Josef Hejzlar, Lisette N. de Senerpont Domis, Jason D. Stockwell, B.W. Ibelings, Rita Adrian, Gaël Dur, R. Iestyn Woolway, James A. Rusak, Lars G. Rudstam, Peeter Nõges, Christian Torsten Seltmann, Pablo Urrutia-Cordero, Piet Verburg, Laurence Carvalho, Karsten Rinke, Dietmar Straile, Shin-ichiro S. Matsuzaki, Hans-Peter Grossart, Tamar Zohary, Marieke A. Frassl, Jonathan P. Doubek, Nasime Janatian, Mikkel René Andersen, University of Vermont [Burlington], Leibniz Institute of Freshwater Ecology and Inland Fisheries (IGB), Institute of Biology at the Department of Biology, Chemistry and Pharmacy, Free University of Berlin (FU), Centre Alpin de Recherche sur les Réseaux Trophiques et Ecosystèmes Limniques (CARRTEL), Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Virginia Tech [Blacksburg], Netherlands Institute of Ecology (NIOO-KNAW), Netherlands Institute of Ecology - NIOO-KNAW (NETHERLANDS), Shizuoka University of Art and Culture (SUAC), Griffith University [Brisbane], State University of New York at Potsdam (SUNY Potsdam), State University of New York (SUNY), Tata Memorial Centre, Helmholtz Zentrum für Umweltforschung = Helmholtz Centre for Environmental Research (UFZ), Fdn Edmund Mach, IASMA Research and Innovation Centre, Limnological Institute, University of Konstanz, Konstanz, Germany, G17AC00044U.S. Geological SurveyNE/J024279/1Natural Environment Research CouncilFondation pour la Recherche sur la BiodiversiteG16AP00087Vermont Water Resources and Lake Studies CenterOIA-1556770U.S. National Science FoundationEF-1702506U.S. National Science FoundationCNS-1737424U.S. National Science FoundationICER-1517823U.S. National Science FoundationDEB-1753639U.S. National Science FoundationH2020-MSCA-ITN-2016MANTELPBA/FS/16/02Irish Government791812European UnionU.S. Department of StateCentre Alpin de Recherche sur les Reseaux Trophiques des Ecosystemes Limniques2017-06421Swedish Research Council, AKWA, Aquatic Ecology (AqE), Institute of Agricultural and Environmental Sciences, Estonian University of Life Sciences, Hydrology and Hydraulic Engineering, Biological stations, Marine Ecosystems Research Group, and Tvärminne Zoological Station

Subjects
0106 biological sciences, 010504 meteorology & atmospheric sciences, Biodiversity & Conservation, Oceanografi, hydrologi och vattenresurser, 01 natural sciences, Oceanography, Hydrology and Water Resources, Water column, ddc:550, functional traits, watershed, General Environmental Science, ddc:333.7-333.9, DIFFERENT CLIMATIC CONDITIONS, changement climatique, Global and Planetary Change, Plan_S-Compliant-TA, Ecology, SPECIES-DIVERSITY, Research Review, lacs, tempête, climate change, Oceanography, WATER-QUALITY, WIND-EXPOSED LAKE, International, 1181 Ecology, evolutionary biology, articles, Biodiversity Conservation, climate change, environmental disturbance, extreme events, functional traits, mixing, nutrients, stability, watershed, Life Sciences & Biomedicine, extreme events, Biogeochemical cycle, environmental disturbance, mixing, nutrients, stability, Storms, Climate Change, Climate change, Environmental Sciences & Ecology, 010603 evolutionary biology, Ecology and Environment, Extreme weather, Rivers, Settore BIO/07 - ECOLOGIA, ddc:570, Phytoplankton, Environmental Chemistry, DISSOLVED ORGANIC-CARBON, CYANOBACTERIAL BLOOM FORMATION, Ecosystem, 0105 earth and related environmental sciences, Functional ecology, Science & Technology, LARGE SHALLOW LAKE, phytoplancton, nutriment, Storm, 15. Life on land, Lakes, Invited Research Review, FUNCTIONAL TRAITS, 13. Climate action, Environmental science, [SDE.BE]Environmental Sciences/Biodiversity and Ecology, THERMAL STRATIFICATION, Surface runoff, Environmental Sciences
Abstract

In many regions across the globe, extreme weather events such as storms have increased in frequency, intensity, and duration due to climate change. Ecological theory predicts that such extreme events should have large impacts on ecosystem structure and function. High winds and precipitation associated with storms can affect lakes via short‐term runoff events from watersheds and physical mixing of the water column. In addition, lakes connected to rivers and streams will also experience flushing due to high flow rates. Although we have a well‐developed understanding of how wind and precipitation events can alter lake physical processes and some aspects of biogeochemical cycling, our mechanistic understanding of the emergent responses of phytoplankton communities is poor. Here we provide a comprehensive synthesis that identifies how storms interact with lake and watershed attributes and their antecedent conditions to generate changes in lake physical and chemical environments. Such changes can restructure phytoplankton communities and their dynamics, as well as result in altered ecological function (e.g., carbon, nutrient and energy cycling) in the short‐ and long‐term. We summarize the current understanding of storm‐induced phytoplankton dynamics, identify knowledge gaps with a systematic review of the literature, and suggest future research directions across a gradient of lake types and environmental conditions., Our understanding of ecosystem‐scale responses to storm events is fragmented, and terminological variability in defining a “storm” hinders resolution of generalizable impacts. We provide a comprehensive synthesis of the interactions between physical properties and biological responses in lakes that demonstrates the context‐dependency of storm impacts; lake/watershed attributes and their antecedent conditions mediate the extent to which storms impact lake ecosystems. We develop a framework which conceptualizes how abrupt, storm‐induced changes in the lake environment influence phytoplankton community dynamics through functional traits, identifies current limitations, and highlights several avenues of research to narrow knowledge gaps in synthetic and interdisciplinary ways.

Published
2020
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2. The effect of exposure to long working hours on ischaemic heart disease A systematic review and meta-analysis from the WHO/ILO Joint Estimates of the Work-related Burden of Disease and Injury

Author

Tracey J. Woodruff, Daniela Vianna Pachito, Frank Pega, Hynek Pikhart, Reiner Rugulies, Alexis Descatha, Akizumi Tsutsumi, Rebecca L. Morgan, Bernd Richter, Peter L. Schnall, Jian Li, Maria-Inti Metzendorf, Paul Landsbergis, Chantal Brisson, Marco M Ferrario, Mattia Roncaioli, Johannes Siegrist, Sergio Iavicoli, Lode Godderis, Xavier Trudel, Grace Sembajwe, Yuka Ujita, Els Clays, University of California (UC), Organisation Mondiale de la Santé / World Health Organization Office (OMS / WHO), Centre de recherche du CHU Sainte-Justine / Research Center of the Sainte-Justine University Hospital [Montreal, Canada], Université de Montréal (UdeM)-CHU Sainte Justine [Montréal], Universiteit Gent = Ghent University (UGENT), Épidémiologie en Santé au Travail et Ergonomie (IRSET-ESTER), Institut de recherche en santé, environnement et travail (Irset), Université d'Angers (UA)-Université de Rennes (UR)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Université d'Angers (UA)-Université de Rennes (UR)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Cohortes épidémiologiques en population (CONSTANCES), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay-Université Paris Cité (UPCité), Université d'Angers (UA)-Université de Rennes (UR)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Universitá degli Studi dell’Insubria = University of Insubria [Varese] (Uninsubria), Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), Istituto Nazionale per l’Assicurazione contro gli Infortuni sul Lavoro [Italian Workers Compensation Authority] (INAIL), State University of New York at Potsdam (SUNY Potsdam), State University of New York (SUNY), Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], McMaster University [Hamilton, Ontario], Universidade Federal de São Paulo, University College of London [London] (UCL), University of Copenhagen = Københavns Universitet (UCPH), University of California [Irvine] (UC Irvine), City University of New York [New York] (CUNY), Kitasato University, University of California [San Francisco] (UC San Francisco), World Health Organization, 5NE11OH010461-03-00, National Institute for Occupational Safety and Health, Jonchère, Laurent, University of California, Centre de recherche du CHU Sainte-Justine [Montreal], CHU Sainte Justine [Montréal]-Université de Montréal (UdeM), Universiteit Gent = Ghent University [Belgium] (UGENT), Université d'Angers (UA)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Université d'Angers (UA)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay-Université de Paris (UP), University of Insubria, Varese, University of Copenhagen = Københavns Universitet (KU), University of California [Irvine] (UCI), University of California [San Francisco] (UCSF), and University of Dusseldorf

Subjects
PROTOCOL, Work, STRESS, 010504 meteorology & atmospheric sciences, EVIDENCE-BASED MEDICINE, [SDV]Life Sciences [q-bio], Myocardial Ischemia, 010501 environmental sciences, 01 natural sciences, law.invention, Randomized controlled trial, Cost of Illness, law, Medicine and Health Sciences, Medicine, Prospective Studies, Prospective cohort study, lcsh:Environmental sciences, General Environmental Science, lcsh:GE1-350, Ischaemic heart disease, 3. Good health, Europe, Occupational Diseases, [SDV] Life Sciences [q-bio], Systematic review, Long working hours, Meta-analysis, CARDIOVASCULAR-DISEASE, Female, HEALTH, Cohort study, ACUTE MYOCARDIAL-INFARCTION, Adolescent, World Health Organization, Work related, Article, RISK-FACTOR, Occupational Exposure, Humans, Risk factor, OVERTIME WORK, METAANALYSIS, 0105 earth and related environmental sciences, business.industry, Long working, SLEEP, Relative risk, business, Demography
Abstract

BACKGROUND: The World Health Organization (WHO) and the International Labour Organization (ILO) are developing Joint Estimates of the work-related burden of disease and injury (WHO/ILO Joint Estimates), with contributions from a large network of experts. Evidence from mechanistic data suggests that exposure to long working hours may cause ischaemic heart disease (IHD). In this paper, we present a systematic review and meta-analysis of parameters for estimating the number of deaths and disability-adjusted life years from IHD that are attributable to exposure to long working hours, for the development of the WHO/ILO Joint Estimates. OBJECTIVES: We aimed to systematically review and meta-analyse estimates of the effect of exposure to long working hours (three categories: 41-48, 49-54 and ≥55 h/week), compared with exposure to standard working hours (35-40 h/week), on IHD (three outcomes: prevalence, incidence and mortality). DATA SOURCES: We developed and published a protocol, applying the Navigation Guide as an organizing systematic review framework where feasible. We searched electronic databases for potentially relevant records from published and unpublished studies, including MEDLINE, Scopus, Web of Science, CISDOC, PsycINFO, and WHO ICTRP. We also searched grey literature databases, Internet search engines and organizational websites; hand-searched reference lists of previous systematic reviews; and consulted additional experts. STUDY ELIGIBILITY AND CRITERIA: We included working-age (≥15 years) workers in the formal and informal economy in any WHO and/or ILO Member State but excluded children (aged

Published
2020
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3. Exploring the Multiligand Binding Specificity of Saposin B Reveals Two Binding Sites

Author

Chloe Zubieta, Britannia M. Smith, Robert P. Doyle, Fadi Bou-Abdallah, Etta Hanlon, Jay Tinklepaugh, Department of Chemistry [Syracuse, NY], Syracuse University, Department of Chemistry [Potsdam], State University of New York at Potsdam (SUNY Potsdam), State University of New York (SUNY)-State University of New York (SUNY), Physiologie cellulaire et végétale (LPCV), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Funding from New York State through the Center for Advanced Systems and Engineering, a NYSTAR-designated center at Syracuse University, Ichor Therapeutics (Lafayette, NY), in-part by the Cottrell College Science Award (ID # 7892) from Research Corporation, and the National Institute of General Medical Sciences of the National Institutes of Health Award R15GM104879, ATIP-Avenir grant, Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

Subjects
0301 basic medicine, leukodystrophy, General Chemical Engineering, 010402 general chemistry, 01 natural sciences, Article, lcsh:Chemistry, Binding site, 03 medical and health sciences, medicine, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Binding selectivity, O-Sulfogalactosylceramide biodegradation, chemistry.chemical_classification, Arylsulfatase, biology, Saponin B, Active site, General Chemistry, medicine.disease, 0104 chemical sciences, Metachromatic leukodystrophy, SapB, 030104 developmental biology, Enzyme, lcsh:QD1-999, Biochemistry, chemistry, biology.protein, Lysosomal protein, Glycoprotein, Human
Abstract

International audience; Saposin B (SapB) is a human lysosomal protein, critical for the degradation of O-sulfogalactosylceramide (sulfatide). SapB binds sulfatide and presents it to the active site of the enzyme arylsulfatase A. Deficiency of SapB leads to fatal activator-deficient metachromatic leukodystrophy. Given the conformational flexibility and the large hydrophobic "pocket" produced upon (physiologically relevant) homodimerization, SapB may have broader substrate diversity than originally thought. Herein, we present evidence using fluorescence spectroscopy and computational docking studies that SapB binds a wide variety of ligands at KD values varying from micromolar to nanomolar, with entropy being the primary driving force. We further demonstrate, for the first time, that SapB has two binding sites that can sequentially (and in a preferred order) accommodate up to two ligands at once.

Published
2017
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4. The Lysosomal Protein Saposin B Binds Chloroquine

Author

Yan Nie, Fadi Bou-Abdallah, Xuelei Lai, Chloe Zubieta, Robert P. Doyle, Matthew R. Mehlenbacher, Brian P. Huta, Department of Chemistry [Syracuse, NY], Syracuse University, Department of Chemistry [Potsdam], State University of New York at Potsdam (SUNY Potsdam), State University of New York (SUNY)-State University of New York (SUNY), European Synchrotron Radiation Facility (ESRF), Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), National Institute of General Medical Sciences of the National Institutes of Health Award Number R15GM104879- ATIP-Avenir program (Joint program of the French National Centre for Scientific Research (CNRS) and the French National Institute of Health and Medical Research (INSERM)), Physiologie cellulaire et végétale (LPCV), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), and Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

Subjects
Models, Molecular, 0301 basic medicine, Cancer therapy, Calorimetry, Biology, Crystallography, X-Ray, Biochemistry, Fluorescence, Saposins, Article, Autoimmune Diseases, 03 medical and health sciences, Lipids degradation, Chloroquine, Drug Discovery, medicine, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, General Pharmacology, Toxicology and Pharmaceutics, Binding site, ComputingMilieux_MISCELLANEOUS, Therapeutic agent, Mecanism of action, Pharmacology, Binding Sites, Molecular Structure, Crystal structure, Organic Chemistry, Saponin B, Isothermal titration calorimetry, Limiting, Hydrogen-Ion Concentration, Lipid degradation, Small molecule, 3. Good health, 030104 developmental biology, Toxicity, Lysosomal protein, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Molecular Medicine, Function (biology), medicine.drug
Abstract

International audience; Chloroquine (CQ) has been widely used in the treatment of malaria since the 1950s, though toxicity and resistance is increasingly limiting its use in the clinic. More recently, CQ is also becoming recognized as an important therapeutic compound for the treatment of autoimmune disorders and has shown activity as an anticancer agent. However, the full extent of CQ pharmacology in humans is still unclear. Herein, we demonstrate that the lysosomal protein saposinB (sapB), critical for select lipid degradation, binds CQ with implications for both CQ function and toxicity. Using isothermal titration calorimetry (ITC) and fluorescence quenching experiments, CQ was shown to bind to the dimeric form of sapB at both pH5.5 and pH7.4 with an average binding affinity of 2.3x10(4)m(-1). X-ray crystallography confirmed this, and the first complete crystal structure of sapB with a bound small molecule (CQ) is reported. The results suggest that sapB might play a role in mitigating CQ-based toxicity and that sapB might itself be overwhelmed by CQ causing impaired lipid degradation.

Published
2016
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5. Heme interplay between IlsA and IsdC: Two structurally different surface proteins from Bacillus cereus

Author

Tyson Terpstra, Didier Lereclus, Elise Abi-Khalil, Gwénaëlle André-Leroux, Fadi Bou-Abdallah, Christina Nielsen-LeRoux, Diego Segond, Mireille Kallassy, André-Leroux, Gwenaelle, MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, department of Biotechnology, Université Saint-Joseph de Beyrouth (USJ), dept. of Chemistry, State University of New York at Potsdam (SUNY Potsdam), State University of New York (SUNY)-State University of New York (SUNY), department of Chemistry, Mathématiques et Informatique Appliquées du Génome à l'Environnement [Jouy-En-Josas] (MaIAGE), Institut National de la Recherche Agronomique (INRA), and Laboratory of Biotechnolog

Subjects
Models, Molecular, Hemeprotein, [SDV]Life Sciences [q-bio], Iron, Molecular Sequence Data, Biophysics, Bacillus cereus, Heme, Leucine-rich repeat, Biochemistry, ILsA NEAT domain, 03 medical and health sciences, chemistry.chemical_compound, hemin binding, hemoglobin, kinetics, LRR domain, Bacterial Proteins, Sequence Analysis, Protein, Amino Acid Sequence, Molecular Biology, 030304 developmental biology, 0303 health sciences, biology, 030306 microbiology, fungi, Isothermal titration calorimetry, biology.organism_classification, Protein Structure, Tertiary, chemistry, Cereus, Hemin, Thermodynamics, Bacteria
Abstract

INRA, MIG, Domaine de Vilvert, F-78352 Jouy en Josas, France : depuis janvier 2015 : INRA, MaIAGE, Domaine de Vilvert, F-78352 Jouy en Josas, France; Iron is an essential element for bacterial growth and virulence. Because of its limited bioavailability in the host, bacteria have adapted several strategies to acquire iron during infection. In the human opportunistic bacteria Bacillus cereus, a surface protein IlsA is shown to be involved in iron acquisition from both ferritin and hemoproteins. IlsA has a modular structure consisting of a NEAT (Near Iron transporter) domain at the N-terminus, several LRR (Leucine Rich Repeat) motifs and a SLH (Surface Layer Homology) domain likely involved in anchoring the protein to the cell surface.METHODS:[b]BACKGROUND:[/b]Isothermal titration calorimetry, UV-Vis spectrophotometry, affinity chromatography and rapid kinetics stopped-flow measurements were employed to probe the binding and transfer of hemin between two different B. cereus surface proteins (IlsA and IsdC).[br/][b]RESULTS:[/b]IlsA binds hemin via the NEAT domain and is able to extract heme from hemoglobin whereas the LRR domain alone is not involved in these processes. A rapid hemin transfer from hemin-containing IlsA (holo-IlsA) to hemin-free IsdC (apo-IsdC) is demonstrated.[br/][b]CONCLUSIONS[/b]:For the first time, it is shown that two different B. cereus surface proteins (IlsA and IsdC) can interact and transfer heme suggesting their involvement in B. cereus heme acquisition.[br/][b]GENERAL SIGNIFICANCE:[/b]An important role for the complete Isd system in heme-associated bacterial growth is demonstrated and new insights into the interplay between an Isd NEAT surface protein and an IlsA-NEAT-LRR protein, both of which appear to be involved in heme-iron acquisition in B. cereus are revealed.

Published
2015
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6. Structural basis for the intracellular regulation of ferritin degradation.

Author

Hoelzgen F, Nguyen TTP, Klukin E, Boumaiza M, Srivastava AK, Kim EY, Zalk R, Shahar A, Cohen-Schwartz S, Meyron-Holtz EG, Bou-Abdallah F, Mancias JD, and Frank GA

Subjects
Humans, Protein Binding, Binding Sites, Iron metabolism, Autophagy, Models, Molecular, HEK293 Cells, Oxidoreductases metabolism, Oxidoreductases chemistry, Oxidoreductases genetics, Proteolysis, Mutation, Ferritins metabolism, Ferritins chemistry, Ferritins genetics, Nuclear Receptor Coactivators metabolism, Nuclear Receptor Coactivators chemistry, Nuclear Receptor Coactivators genetics, Cryoelectron Microscopy
Abstract

The interaction between nuclear receptor coactivator 4 (NCOA4) and the iron storage protein ferritin is a crucial component of cellular iron homeostasis. The binding of NCOA4 to the FTH1 subunits of ferritin initiates ferritinophagy-a ferritin-specific autophagic pathway leading to the release of the iron stored inside ferritin. The dysregulation of NCOA4 is associated with several diseases, including neurodegenerative disorders and cancer, highlighting the NCOA4-ferritin interface as a prime target for drug development. Here, we present the cryo-EM structure of the NCOA4-FTH1 interface, resolving 16 amino acids of NCOA4 that are crucial for the interaction. The characterization of mutants, designed to modulate the NCOA4-FTH1 interaction, is used to validate the significance of the different features of the binding site. Our results explain the role of the large solvent-exposed hydrophobic patch found on the surface of FTH1 and pave the way for the rational development of ferritinophagy modulators., (© 2024. The Author(s).)

Published
2024
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7. Calibration of mammalian skeletal muscle Ca 2+ transients recorded with the fast Ca 2+ dye Mag-Fluo-4.

Author

Milán AF, Rincón OA, Arango LB, Reutovich AA, Smith GL, Giraldo MA, Bou-Abdallah F, and Calderón JC

Subjects
Animals, Fluorescent Dyes chemistry, Fura-2 chemistry, Fura-2 metabolism, Male, Mice, Mice, Inbred C57BL, Muscle, Skeletal chemistry, Thermodynamics, Calcium metabolism, Fluorescent Dyes metabolism, Fura-2 analogs & derivatives, Muscle, Skeletal metabolism
Abstract

Background: Mag-Fluo-4 is increasingly employed for studying Ca 2+ signaling in skeletal muscle; however, the lack of information on the Ca 2+ -Mag-Fluo-4 reaction limits its wider usage., Methods: Fluorescence and isothermal titration calorimetry (ITC) experiments were performed to determine the binding stoichiometry (n) and thermodynamics (enthalpy (ΔH) and entropy (ΔS) changes), as well as the in vitro and in situ K d of the Ca 2+ -Mag-Fluo-4 reaction. Rate constants (k on , k off ), fluorescence maximum (F max ), minimum (F min ), and the dye compartmentalization were also estimated. Experiments in cells used enzymatically dissociated flexor digitorum brevis fibres of C57BL6, adult mice, loaded at room temperature for 8 min, with 6 μM Mag-Fluo-4, AM, and permeabilized with saponin or ionomycin. All measurements were done at 20 °C., Results: The in vitro fluorescence assays showed a binding stoichiometry of 0.5 for the Ca 2+ /Mag-Fluo-4 (n = 5) reaction. ITC results (n = 3) provided ΔH and ΔS values of 2.3 (0.7) kJ/mol and 97.8 (5.9) J/mol.K, respectively. The in situ K d was 1.652 × 10 5 μM 2 (n = 58 fibres, R 2  = 0.99). With an F max of 150.9 (8.8) A.U. (n = 8), F min of 0.14 (0.1) A.U. (n = 10), and ΔF of Ca 2+ transients of 8.4 (2.5) A.U. (n = 10), the sarcoplasmic [Ca 2+ ] peak reached 22.5 (7.8) μM. Compartmentalized dye amounted to only 1.1 (0.7)% (n = 10)., Conclusions: Two Mag-Fluo-4 molecules coalesce around one Ca 2+ ion, in an entropy-driven, very low in situ affinity reaction, making it suitable to reliably track the kinetics of rapid muscle Ca 2+ transients., General Significance: Our results may be relevant to the quantitative study of Ca 2+ kinetics in many other cell types., (Copyright © 2021 Elsevier B.V. All rights reserved.)

Published
2021
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