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5. Endocannabinoid regulation of inward rectifier potassium (Kir) channels.

Author

Mayar, Sultan, Borbuliak, Mariia, Zoumpoulakis, Andreas, Bouceba, Tahar, Labonté, Madeleine M., Ahrari, Ameneh, Sinniah, Niveny, Memarpoor-Yazdi, Mina, Vénien-Bryan, Catherine, Tieleman, D. Peter, and D'Avanzo, Nazzareno

Subjects
SURFACE plasmon resonance, PROTEIN-lipid interactions, IONS, MOLECULAR dynamics, LIGANDS (Biochemistry), POTASSIUM channels, CANNABINOID receptors, ION channels
Abstract

The inward rectifier potassium channel Kir2.1 (KCNJ2) is an important regulator of resting membrane potential in both excitable and non-excitable cells. The functions of Kir2.1 channels are dependent on their lipid environment, including the availability of PI(4,5)P2, secondary anionic lipids, cholesterol and long-chain fatty acids acyl coenzyme A (LC-CoA). Endocannabinoids are a class of lipids that are naturally expressed in a variety of cells, including cardiac, neuronal, and immune cells. While these lipids are identified as ligands for cannabinoid receptors there is a growing body of evidence that they can directly regulate the function of numerous ion channels independently of CBRs. Here we examine the effects of a panel of endocannabinoids on Kir2.1 function and demonstrate that a subset of endocannabinoids can alter Kir2.1 conductance to varying degrees independently of CBRs. Using computational and Surface plasmon resonance analysis, endocannabinoid regulation of Kir2.1 channels appears to be the result of altered membrane properties, rather than through direct protein-lipid interactions. Furthermore, differences in endocannabinoid effects on Kir4.1 and Kir7.1 channels, indicating that endocannabinoid regulation is not conserved among Kir family members. These findings may have broader implications on the function of cardiac, neuronal and/or immune cells. [ABSTRACT FROM AUTHOR]

Published
2024
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6. Chlordecone-Induced Hepatotoxicity and Fibrosis are Mediated by the Proteasomal Degradation of Septins

Author

Léger, Thibaut, primary, Alilat, Sarah, additional, Ferron, Pierre-Jean, additional, Dec, Léonie, additional, Bouceba, Tahar, additional, Lanceleur, Rachelle, additional, Huet, Sylvie, additional, Devriendt-Renault, Yoann, additional, Parinet, Julien, additional, Clément, Bruno, additional, Fessard, Valérie, additional, and Le Hégarat, Ludovic, additional

Published
2024
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10. A receptor-independent signaling pathway for BDNF

Author

Fath, Julia, primary, Brouillard, Franck, additional, Cabaye, Alexandre, additional, Claverie, Damien, additional, Nuss, Philippe, additional, Poillerat, Victoria, additional, Chwetzoff, Serge, additional, Bouceba, Tahar, additional, Bouvier, Elodie, additional, Salameh, Myriam, additional, Molet, Jenny, additional, Padilla-Ferrer, Aïda, additional, Couvert, Philippe, additional, Acher, Francine, additional, Golinelli-Cohen, Marie-Pierre, additional, Chassaing, Gérard, additional, Trugnan, Germain, additional, Bernard, Christophe, additional, Benoliel, Jean-Jacques, additional, and Becker, Chrystel, additional

Published
2022
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22. Reverse Immunology Approach to Define a New HIV-gp41-Neutralizing Epitope

Author

Dorgham, Karim, primary, Pietrancosta, Nicolas, additional, Affoune, Amel, additional, Lucar, Olivier, additional, Bouceba, Tahar, additional, Chardonnet, Solenne, additional, Pionneau, Cedric, additional, Piesse, Christophe, additional, Sterlin, Delphine, additional, Guardado-Calvo, Pablo, additional, Karoyan, Philippe, additional, Debré, Patrice, additional, Gorochov, Guy, additional, and Vieillard, Vincent, additional

Published
2019
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23. Insight into the mechanism of action of temporin-SHa, a new broad-spectrum antiparasitic and antibacterial agent

Author

Raja, Zahid, André, Sonia, Abbassi, Feten, Humblot, Vincent, Lequin, Olivier, Bouceba, Tahar, Correia, Isabelle, Casale, Sandra, Foulon, Thierry, Sereno, Denis, Oury, Bruno, Ladram, Ali, Biosynthèse des Signaux Peptidiques [IBPS] (IBPS-BIOSIPE), Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Réactivité de Surface (LRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Laboratoire des biomolécules (LBM UMR 7203), Université Pierre et Marie Curie - Paris 6 (UPMC)-Département de Chimie - ENS Paris, École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Ingénierie des protéines, PCR, Interaction Moléculaires [IBPS] (IBPS-IPIM), Service de Biochimie, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Bicêtre, Maladies infectieuses et vecteurs : écologie, génétique, évolution et contrôle (MIVEGEC), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud]), Interactions hôtes-vecteurs-parasites-environnement dans les maladies tropicales négligées dues aux trypanosomatides (UMR INTERTRYP), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut de Recherche pour le Développement (IRD)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Université de Bordeaux (UB), ANR-11-IDEX-0004,SUPER,Sorbonne Universités à Paris pour l'Enseignement et la Recherche(2011), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Département de Chimie - ENS Paris, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Pierre et Marie Curie - Paris 6 (UPMC), Université de Bordeaux (UB)-Institut de Recherche pour le Développement (IRD)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Université de Lyon-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)

Subjects
Life Cycles, Cell Membrane Permeability, Time Factors, Staphylococcus, Cell Membranes, Drug Evaluation, Preclinical, lcsh:Medicine, Apoptosis, Protozoology, Pathology and Laboratory Medicine, Membrane Potentials, Medicine and Health Sciences, Staphylococcus Aureus, lcsh:Science, Protozoans, Leishmania, Membrane Potential, Mitochondrial, Cell Death, Bacterial Pathogens, Anti-Bacterial Agents, Cell Processes, Medical Microbiology, Protozoan Life Cycles, Cellular Structures and Organelles, Pathogens, Research Article, Trypanosoma, Leishmania Infantum, Antiprotozoal Agents, DNA Fragmentation, Microbiology, Cell Line, stomatognathic system, Microbial Control, Drug Resistance, Bacterial, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Gram Negative Bacteria, Microbial Pathogens, Unilamellar Liposomes, Pharmacology, Bacteria, Dose-Response Relationship, Drug, Promastigotes, lcsh:R, Organisms, Biology and Life Sciences, Bacteriology, Cell Biology, DNA, Protozoan, Parasitic Protozoans, Ampicillin, lcsh:Q, Antimicrobial Resistance, Developmental Biology, Antimicrobial Cationic Peptides
Abstract

International audience; Antimicrobial peptides (AMPs) are promising drugs to kill resistant pathogens. In contrast to bacteria, protozoan parasites, such as Leishmania, were little studied. Therefore, the antiparasitic mechanism of AMPs is still unclear. In this study, we sought to get further insight into this mechanism by focusing our attention on temporin-SHa (SHa), a small broad-spectrum AMP previously shown to be active against Leishmania infantum. To improve activity, we designed analogs of SHa and compared the antibacterial and antiparasitic mechanisms. [K3]SHa emerged as a highly potent compound active against a wide range of bacteria, yeasts/fungi, and trypanosomatids (Leishmania and Trypanosoma), with leishmanicidal intramacrophagic activity and efficiency toward antibiotic-resistant strains of S. aureus and antimony-resistant L. infantum. Multipassage resistance selection demonstrated that temporins-SH, particularly [K3]SHa, are not prone to induce resistance in Escherichia coli. Analysis of the mode of action revealed that bacterial and parasite killing occur through a similar membranolytic mechanism involving rapid membrane permeabilization and depolarization. This was confirmed by high-resolution imaging (atomic force microscopy and field emission gun-scanning electron microscopy). Multiple combined techniques (nuclear magnetic resonance, surface plasmon resonance, differential scanning calorimetry) allowed us to detail peptide-membrane interactions. [K3]SHa was shown to interact selectively with anionic model membranes with a 4-fold higher affinity (KD = 3 x 10−8 M) than SHa. The amphipathic α-helical peptide inserts in-plane in the hydrophobic lipid bilayer and disrupts the acyl chain packing via a detergent-like effect. Interestingly, cellular events, such as mitochondrial membrane depolarization or DNA fragmentation, were observed in L. infantum promastigotes after exposure to SHa and [K3]SHa at concentrations above IC50. Our results indicate that these temporins exert leishmanicidal activity via a primary membranolytic mechanism but can also trigger apoptotis-like death. The many assets demonstrated for [K3]SHa make this small analog an attractive template to develop new antibacterial/antiparasitic drugs.

Published
2017
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24. A Functional Role for the Monomethylated Gln-51 and Lys-53 Residues of the 49GGQTK53 Motif of eL42 from Human 80S Ribosomes

Author

Eustache, Stéphanie, Créchet, Jean-Bernard, Bouceba, Tahar, Nakayama, Jun-ichi, Tanaka, Mayo, Suzuki, Mieko, Woisard, Anne, Tuffery, Pierre, Baouz, Soria, Hountondji, Codjo, Enzymologie de l'ARN, Université Pierre et Marie Curie - Paris 6 (UPMC), Ingénierie des protéines, PCR, Interaction Moléculaires [IBPS] (IBPS-IPIM), Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
eL42 protein, [SDV]Life Sciences [q-bio], education, eL42/human translation termination factor, 28S rRNA/binding assays, Human 80S ribosomes/GGQTK motif, eL42/monomethylated Gln-51, Article, eRF1/tRNA, Lys-53 residues, Biacore
Abstract

Background: We have previously demonstrated that the eukaryote-specific ribosomal protein eL42 of the human 80S ribosome contains seven monomethylated residues, among which are the Gln-51 and Lys-53 residues contained in the 47GFGGQTK53 sequence conserved in all eukaryotic 80S ribosomes. This sequence contains the methylated and universally conserved GGQ motif common for all class-1 translation termination factors responsible for stop codon recognition and for triggering the hydrolysis of the P site-bound peptidyl-tRNA. We have also recently reported a model of ribosomal ternary eL42-tRNA-eRF1 complex where specific regions of all three macromolecules (the comparably flexible GGQ domains of eRF1 and eL42 and the CCA-arm of tRNA) are involved in interactions. Method: Here, we have studied the interactions between recombinant eL42 and eRF1 proteins and the tRNA substrate by means of the Biacore assay, using the wild-type eL42 protein, the eL42-Δ(GGQTK) mutant (the eL42 protein whose GGQTK motif has been deleted), the single Q51E and K53Q mutants (eL42-Q51E and eL42-K53Q, respectively), as well as the double Q51A/K53A mutant (eL42-Q51A/K53A). Results: Our results show that the monomethylated Gln-51 and Lys-53 residues contained in the 47GFGGQTK53 sequence of eL42 and the monomethylated GGQ motif of eRF1 represents the sites of interaction between these two proteins through hydrophobic contacts between methyl groups. We also demonstrate that the interactions between eL42 and tRNA or 28S rRNA are characterized by strong binding affinities (KD values in the nanomolar or picomolar range, respectively) which argue for specific interactions. Strong interactions between eL42 and tRNA are likely to be responsible for the decrease in the poly(U)-dependent poly(Phe) synthesis activity of human 80S or E. coli 70S ribosomes in the presence of added human recombinant eL42. It is proposed that the decrease of the activity of the ribosome is caused by the sequestration of the substrate Phe-tRNAPhe by the added eL42 protein. Conclusion: Interactions between the monomethylated Gln-51 and Lys-53 residues of the 49GGQTK53 motif of the human eL42 protein and the methylated GGQ motif of eRF1 are likely to play a functional role on translating human 80S ribosomes.

Published
2017
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26. Functional characterization of a humanPOU1F1mutation associated with isolated growth hormone deficiency: a novel etiology for IGHD

Author

Sobrier, Marie-Laure, primary, Tsai, Yu-Cheng, additional, Pérez, Christelle, additional, Leheup, Bruno, additional, Bouceba, Tahar, additional, Duquesnoy, Philippe, additional, Copin, Bruno, additional, Sizova, Daria, additional, Penzo, Alfredo, additional, Stanger, Ben Z., additional, Cooke, Nancy E., additional, Liebhaber, Stephen A., additional, and Amselem, Serge, additional

Published
2015
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27. Mechanisms of Site-Specific Functions of Focal Adhesion Kinase

Author

Brami-Cherrier, Karen, primary, Gervasi, Nicolas, additional, Arsenieva, Diana, additional, Boutterin, Marie-Claude, additional, Ortega, Alvaro, additional, Seantier, Bastian, additional, Gasmi, Laila, additional, Bouceba, Tahar, additional, Noble, Martin E.M., additional, Girault, Jean-Antoine, additional, and Arold, Stefan T., additional

Published
2013
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28. New Partners in Regulation of Gene Expression: The Enhancer of Trithorax and Polycomb Corto Interacts with Methylated Ribosomal Protein L12 Via Its Chromodomain

Author

Coléno-Costes, Anne, primary, Jang, Suk Min, additional, de Vanssay, Augustin, additional, Rougeot, Julien, additional, Bouceba, Tahar, additional, Randsholt, Neel B., additional, Gibert, Jean-Michel, additional, Le Crom, Stéphane, additional, Mouchel-Vielh, Emmanuèle, additional, Bloyer, Sébastien, additional, and Peronnet, Frédérique, additional

Published
2012
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30. A New Vesicular Scaffolding Complex Mediates the G-Protein-Coupled 5-HT1A Receptor Targeting to Neuronal Dendrites.

Author

Awabdh, Sana Al, Miserey-Lenkei, Stéphanie, Bouceba, Tahar, Masson, Justine, Kano, Fumi, Marinach-Patrice, Carine, Hamon, Michel, Emerit, Michel Boris, and Darmon, Michéle

Subjects
SCAFFOLD proteins, G protein coupled receptors, SEROTONIN receptors, TARGETED drug delivery, DENDRITES, BRAIN function localization, GENE expression, LABORATORY rats
Abstract

Although essential for their neuronal function, the molecular mechanisms underlying the dendritic targeting of serotonin G-proteincoupled receptors are poorly understood. Here, we characterized a Yif1B-dependent vesicular scaffolding complex mediating the intracellular traffic of the rat 5-HT1A receptor (5-HT1AR) toward dendrites. By combining directed mutagenesis, GST-pull down, and surface plasmon resonance, we identified a tribasic motif in the C-tail of the 5-HT1AR on which Yif1B binds directly with high affinity (KD37 nM). Moreover, we identified Yip1A, Rab6, and Kif5B as new partners of the 5-HT1AR/Yif1B complex, and showed that their expression in neurons is also crucial for the dendritic targeting of the 5-HT1AR. Live videomicroscopy revealed that 5-HT1AR, Yif1B, Yip1A, and Rab6 traffic in vesicles exiting the soma toward the dendritic tree, and also exhibit bidirectional motions, sustaining their role in 5-HT1AR dendritic targeting. Hence, we propose a new trafficking pathway model in which Yif1B is the scaffold protein recruiting the 5-HT1AR in a complex including Yip1A and Rab6, with Kif5B and dynein as two opposite molecular motors coordinating the traffic of vesicles along dendritic microtubules. This targeting pathway opens new insights for G-protein-coupled receptors trafficking in neurons. [ABSTRACT FROM AUTHOR]

Published
2012
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31. Trichoplaxin - A new membrane-active antimicrobial peptide from placozoan cDNA

Author

Monica Benincasa, Juraj Simunić, Dražen Petrov, Nédia Kamech, Tahar Bouceba, Davor Juretić, Ingénierie des protéines, PCR, Interaction Moléculaires [IBPS] (IBPS-IPIM), Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Croatian Ministry of Science, Education and Sports [177-1770495-0476], French government, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Simunić, Juraj, Petrov, Dražen, Bouceba, Tahar, Kamech, Nédia, Benincasa, Monica, and Juretić, Davor

Subjects
Anti-Infective Agent, Secondary, [SDV]Life Sciences [q-bio], Peptide, Biochemistry, Protein Structure, Secondary, chemistry.chemical_compound, Anti-Infective Agents, EST database, Models, Complementary, Candida, chemistry.chemical_classification, Expressed sequence tag, Antimicrobial Cationic Peptide, Tumor, Membrane, Bacterial, U937 Cells, Antimicrobial, Peptide–membrane interaction, U937 Cell, Antimicrobial peptide, Lead compound, Peptide-membrane interaction, Trichoplax adhaeren, Human, Signal peptide, DNA, Bacterial, Protein Structure, DNA, Complementary, Molecular Sequence Data, Biophysics, Biology, Gram-Positive Bacteria, Models, Biological, Cell Line, Complementary DNA, Cell Line, Tumor, Surface plasmon resonance, Gram-Negative Bacteria, Animals, Humans, Placozoa, Propidium iodide, Amino Acid Sequence, antimicrobial peptide, Trichoplax adhaerens, selectivity index, surface plasmon resonance, peptide-membrane interaction, Kinetic, Membranes, Animal, DNA, Cell Biology, Selectivity index, Biological, Molecular biology, Antimicrobial Cationic Peptides, Kinetics, Rats, Sequence Alignment, Surface Plasmon Resonance, chemistry, Rat
Abstract

International audience; A method based on the use of signal peptide sequences from antimicrobial peptide (AMP) precursors was used to mine a placozoa expressed sequence tag database and identified a potential antimicrobial peptide from Trichoplax adhaerens. This peptide, with predicted sequence FFGRLKSVWSAVKHGWKAAKSR is the first AMP from a placozoan species, and was named trichoplaxin. It was chemically synthesized and its structural properties, biological activities and membrane selectivity were investigated. It adopts an a-helical structure in contact with membrane-like environments and is active against both Gram-negative and Gram-positive bacterial species (including MRSA), as well as yeasts from the Candida genus. The cytotoxic activity, as assessed by the haemolytic activity against rat erythrocytes, U937 cell permeabilization to propidium iodide and MCF7 cell mitochondrial activity, is significantly lower than the antimicrobial activity. In tests with membrane models, trichoplaxin shows high affinity for anionic prokaryote-like membranes with good fit in kinetic studies. Conversely, there is a low affinity for neutral eukaryote-like membranes and absence of a dose dependent response. With high selectivity for bacterial cells and no homologous sequence in the UniProt, trichoplaxin is a new potential lead compound for development of broad-spectrum antibacterial drugs.

Published
2014
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32. A Functional Role for the Monomethylated Gln-51 and Lys-53 Residues of the 49GGQTK53 Motif of eL42 from Human 80S Ribosomes.

Author

Eustache S, Créchet JB, Bouceba T, Nakayama JI, Tanaka M, Suzuki M, Woisard A, Tuffery P, Baouz S, and Hountondji C

Abstract

Background: We have previously demonstrated that the eukaryote-specific ribosomal protein eL42 of the human 80S ribosome contains seven monomethylated residues, among which are the Gln-51 and Lys-53 residues contained in the 47GFGGQTK53 sequence conserved in all eukaryotic 80S ribosomes. This sequence contains the methylated and universally conserved GGQ motif common for all class-1 translation termination factors responsible for stop codon recognition and for triggering the hydrolysis of the P site-bound peptidyl-tRNA. We have also recently reported a model of ribosomal ternary eL42-tRNA-eRF1 complex where specific regions of all three macromolecules (the comparably flexible GGQ domains of eRF1 and eL42 and the CCA-arm of tRNA) are involved in interactions., Method: Here, we have studied the interactions between recombinant eL42 and eRF1 proteins and the tRNA substrate by means of the Biacore assay, using the wild-type eL42 protein, the eL42-Δ(GGQTK) mutant (the eL42 protein whose GGQTK motif has been deleted), the single Q51E and K53Q mutants (eL42-Q51E and eL42-K53Q, respectively), as well as the double Q51A/K53A mutant (eL42-Q51A/K53A)., Results: Our results show that the monomethylated Gln-51 and Lys-53 residues contained in the 47GFGGQTK53 sequence of eL42 and the monomethylated GGQ motif of eRF1 represents the sites of interaction between these two proteins through hydrophobic contacts between methyl groups. We also demonstrate that the interactions between eL42 and tRNA or 28S rRNA are characterized by strong binding affinities ( K D values in the nanomolar or picomolar range, respectively) which argue for specific interactions. Strong interactions between eL42 and tRNA are likely to be responsible for the decrease in the poly(U)-dependent poly(Phe) synthesis activity of human 80S or E. coli 70S ribosomes in the presence of added human recombinant eL42. It is proposed that the decrease of the activity of the ribosome is caused by the sequestration of the substrate Phe-tRNA Phe by the added eL42 protein., Conclusion: Interactions between the monomethylated Gln-51 and Lys-53 residues of the 49GGQTK53 motif of the human eL42 protein and the methylated GGQ motif of eRF1 are likely to play a functional role on translating human 80S ribosomes.

Published
2017
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