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Accueil > Départements > Biologie Cellulaire > Anne-Marie TASSIN : Biogénese et fonction des structures centriolaires et ciliaires

Publications de l’équipe

2017


  • A. Aubusson-Fleury, G. Balavoine, M. Lemullois, K. Bouhouche, J. Beisson, et F. Koll, « Centrin diversity and basal body patterning across evolution: new insights from Paramecium », Biology Open, 2017.
    Résumé : First discovered in unicellular eukaryotes, centrins play crucial roles in basal body duplication and anchoring mechanisms. While the evolutionary status of the founding members of the family, Centrin2/Vfl2 and Centrin3/cdc31 has long been investigated, the evolutionary origin of other members of the family has received less attention. Using a phylogeny of ciliate centrins, we identify two other centrin families, the ciliary centrins and the centrins present in the contractile filaments (ICL centrins). In this paper, we carry on the functional analysis of still not well known centrins, the ICL1e subfamily identified in Paramecium, and show their requirement for correct basal body anchoring through interactions with Centrin2 and Centrin3. Using Paramecium as well as an Eukaryote-wide sampling of centrins from completely sequenced genomes, we revisited the evolutionary story of centrins. Their phylogeny shows that the centrins associated with the ciliate contractile filaments are widespread in eukaryotic lineages and could be as ancient as Centrin2 and Centrin3.
    Mots-clés : basal body anchoring, basal body assembly, BIOCELL, BIOCIL, centrin evolution, Ciliary centrins, ciliated epithelia polarity.


  • H. Bengueddach, M. Lemullois, A. Aubusson-Fleury, et F. Koll, « Basal body positioning and anchoring in the multiciliated cell Paramecium tetraurelia: roles of OFD1 and VFL3 », Cilia, vol. 6, nᵒ 1, 2017.

  • M. J. Domingues, J. Martinez-Sanz, L. Papon, L. Larue, L. Mouawad, et J. Bonaventure, « Structure-based mutational analysis of ICAT residues mediating negative regulation of β-catenin co-transcriptional activity », PloS One, vol. 12, nᵒ 3, p. e0172603, 2017.
    Résumé : ICAT (Inhibitor of β-CAtenin and TCF) is a small acidic protein that negatively regulates β-catenin co-transcriptional activity by competing with TCF/LEF factors in their binding to β-catenin superhelical core. In melanoma cells, ICAT competes with LEF1 to negatively regulate the M-MITF and NEDD9 target genes. The structure of ICAT consists of two domains: the 3-helix bundle N-terminal domain binds to β-catenin Armadillo (Arm) repeats 10-12 and the C-terminal tail binds to Arm repeats 5-9. To elucidate the structural mechanisms governing ICAT/β-catenin interactions in melanoma cells, three ICAT residues Y15, K19 and V22 in the N-terminal domain, contacting hydrophobic β-catenin residue F660, were mutated and interaction was assessed by immunoprecipitation. Despite the moderate hydrophobicity of the contact, its removal completely abolished the interaction. In the ICAT C-terminal tail consensus sequence, neutralization of the electrostatic interactions between residues D66, E75 and β-catenin residues K435, K312, coupled to deletion of the hydrophobic contact between F71 and β-catenin R386, markedly reduced, but failed to abolish the ICAT-mediated negative regulation of M-MITF and NEDD9 promoters. We conclude that in melanoma cells, anchoring of ICAT N-terminal domain to β-catenin through the hook made by residue F660, trapped in the pincers formed by ICAT residues Y15 and V22, is crucial for stabilizing the ICAT/β-catenin complex. This is a prerequisite for binding of the consensus peptide to Arm repeats 5-9 and competition with LEF1. Differences between ICAT and LEF1 in their affinity for β-catenin may rely on the absence in ICAT of hydrophilic residues between D66 and F71.
    Mots-clés : BIOCELL, BIOCIL.

  • L. Shi, K. France, O. Arnaiz, et J. Cohen, « The Ciliary Protein IFT57 in the Macronucleus of Paramecium », The Journal of Eukaryotic Microbiology, 2017.
    Résumé : The intraflagellar transport IFT57 protein is essential for ciliary growth and maintenance. Also known as HIPPI, human IFT57 can be translocated to the nucleus via a molecular partner of the Huntingtin, Hip1, inducing gene expression changes. In Paramecium tetraurelia, we identified four IFT57 genes forming two subfamilies IFT57A/B and IFT57C/D arising from whole genome duplications. The depletion of proteins of the two subfamilies induced ciliary defects and IFT57A and IFT57C localized in basal bodies and cilia. We observed that IFT57A, but not IFT57C, is also present in the macronucleus and able to traffic toward the developing anlage during autogamy. Analysis of chimeric IFT57A-IFT57C-GFP-tagged proteins allowed us to identify a region of IFT57A necessary for nuclear localization. We studied the localization of the unique IFT57 protein of Paramecium caudatum, a species, which diverged from Paramecium tetraurelia before the whole genome duplications. The Paramecium caudatum IFT57C protein was excluded from the nucleus. We also analyzed whether the overexpression of IFT57A in Paramecium could affect gene transcription as the human protein does in HeLa cells. The expression of some genes was indeed affected by overexpression of IFT57A, but the set of affected genes poorly overlaps the set of genes affected in human cells. This article is protected by copyright. All rights reserved.
    Mots-clés : ANGE, BIOCELL, BIOCIL, cilia, DBG, IFT57 /HIPPI, intraflagellar transport (IFT), Macronucleus, Paramecium.

2015

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2014
Eguether T, Ermolaeva MA, Zhao Y, Bonnet MC, Jain A, Pasparakis M, Courtois G, Tassin AM. (2014) The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells. Nature Communications. 2014 Aug 19 ;5:4585. PMID : 25134987.

2013
Aubusson-Fleury A, Bricheux G, Damaj R, Lemullois M, Coffe G, Donnadieu F, Koll F, Viguès B, Bouchard P. (2013) Epiplasmins and epiplasm in paramecium : the building of a submembraneous cytoskeleton. Protist. 164, 451-69. PMID : 23837920.

2012
Jerka-Dziadosz, M., Koll, F., Włoga, D., Gogendeau, D., Garreau de Loubresse, N., Ruiz, F., Fabczak, S., Beisson, J. A Centrin3-dependent, transient appendage of the mother basal body guides the positioning of the daughter basal body in Paramecium. Protist. 2012 Dec 20. doi:pii : S1434-4610(12)00121-6.10.1016/j.protis.2012.11.003. PMID : 23261281.
Aubusson-Fleury, A., Lemullois, M., de Loubresse, N.G., Laligné, C., Cohen, J., Rosnet, O., Jerka-Dziadosz, M., Beisson, J., and Koll, F. (2012). The conserved centrosomal protein FOR20 is required for assembly of the transition zone and basal body docking at the cell surface. J Cell Sci 125, 4395-4404. PMID : 22718349.
Valentine, M.S., Rajendran, A., Yano, J., Weeraratne, S.D., Beisson, J., Cohen, J., Koll, F., & Van Houten, J. (2012). Paramecium BBS genes are key to channel function in motile cilia. Cilia 1:16. doi : 10.1186/2046-2530-1-16. PMID : 23351336.

2011
Gogendeau, D., Hurbain, I., Raposo, G., Cohen, J., Koll, F., Basto, R. (2011) Sas-4 proteins are required during basal body duplication in Paramecium. Mol Biol Cell, 22 (7) 1035-44. PMID : 21289083.

2010
Guichard P, Chrétien D, Marco S, Tassin AM. (2010). Procentriole assembly revealed by cryo-electron tomography. EMBO J. 29:1565-72. PMID : 20339347.
Arnaiz, O., Gout, J-F., Bétermier, M., Bouhouche, K., Cohen, J., Duret, L., Kapusta, A., Meyer, E. and Sperling, L. (2010) Gene expression in a paleopolyploid : a transcriptome resource for the ciliate Paramecium tetraurelia. BMC Genomics, 11:547. PMID : 20932287.
Jerka-Dziadosz, M., Gogendeau, D., Klotz, C., Cohen, J., Beisson, J. and Koll, F. (2010) Basal body duplication in Paramecium : the key role of Bld10 in assembly and stability of the cartwheel. Cytoskeleton (Hoboken) 67 (3) 161-71. PMID : 20217679.
Laligné, C., Klotz, C., Garreau de Loubresse, N., Lemullois, M., Hori, M., Laurent, F.-X., Papon, J.-F., Louis, B., Cohen, J. and Koll, F. (2010) Bug22p, a conserved centrosomal/ciliary protein also present in higher plants is required for an effective ciliary stroke in Paramecium. Eukaryot Cell, 9 (4) 645-55. PMID : 20118210.

2009
Arnaiz, O., Malinowska, A., Klotz, C., Sperling, L., Dadlez, M., Koll, F. & Cohen J. 2009. Cildb : a knowledgebase for centrosomes and cilia. Database, doi:10.1093/database/bap022. PMID : 20428338.

In collaboration
Singh DP, Saudemont B, Guglielmi G, Arnaiz O, Goût JF, Prajer M, Potekhin A, Przybòs E, Aubusson-Fleury A, Bhullar S, Bouhouche K, Lhuillier-Akakpo M, Tanty V, Blugeon C, Alberti A, Labadie K, Aury JM, Sperling L, Duharcourt S, Meyer E. (2014) Genome-defence small RNAs exapted for epigenetic mating-type inheritance. Nature 509, 447-52. PMID : 24805235.
Kutomi, O., Hori, M., Ishida, M., Tominaga, T., Kamachi, H., Koll, F., Cohen, J., Yamada, N., and Noguchi, M. (2012). Outer dynein arm light chain 1 is essential for controlling the ciliary response to cyclic AMP in Paramecium tetraurelia. Eukaryot Cell 11, 645-653. PMID : 22427431.

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