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Izard, T.
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Izard, T.

Faculty Member
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Positions

  • 2017 - Professor (Joint Appointment), Immunology and Microbiology , Scripps Research
  • 2017 - Professor, Integrative Structural and Computational Biology (ISCB) , Scripps Research
  • 2007 - Faculty Member, Skaggs Graduate School of Chemical and Biological Sciences , Scripps Research
  • 2007 - 2017 Associate Professor Tenure (Joint Appointment), Immunology and Microbiology , Scripps Research
  • 2007 - 2017 Associate Professor Tenure, Integrative Structural and Computational Biology (ISCB) , Scripps Research
Dr. Izard studies the structural dynamics of signaling mediators of adhesion junctions.

Research Areas research areas

  • Cancer (UMLS)
  • Heart Disease (UMLS)

Websites

  • T. Izard, Ph.D.
  • Izard Laboratory
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Publications

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  • academic article

    • Lietha, D., Izard, T. Roles of Membrane Domains in Integrin-Mediated Cell Adhesion International Journal of Molecular Sciences  2020 21  DOI:10.3390/ijms21155531  PMID:32752284  PMCID:PMC7432473
    • Janiszewska, M., Primi, M. C., Izard, T. Cell adhesion in cancer: Beyond the migration of single cells Journal of Biological Chemistry  2020 295:2495-2505  DOI:10.1074/jbc.REV119.007759  PMID:31937589  PMCID:PMC7039572
    • Rangarajan, E. S., Primi, M. C., Colgan, L. A., Chinthalapudi, K., Yasuda, R., Izard, T. A distinct talin2 structure directs isoform specificity in cell adhesion Journal of Biological Chemistry  2020 295:12885-12899  DOI:10.1074/jbc.RA119.010789  PMID:32605925  PMCID:PMC7489915
    • Valencia-Gallardo, C., Bou-Nader, C., Aguilar-Salvador, D. T., Carayol, N., Quenech'Du, N., Pecqueur, L., Park, H., Fontecave, M., Izard, T., Van Nhieu, G. T. Shigella IpaA binding to talin stimulates filopodial capture and cell adhesion Cell Reports  2019 26:921-932  DOI:10.1016/j.celrep.2018.12.091  PMID:30673614
    • Mediouni, S., Chinthalapudi, K., Ekka, M. K., Usui, I., Jablonski, J. A., Clementz, M. A., Mousseau, G., Nowak, J., Macherla, V. R., Beverage, J. N., Esquenazi, E., Baran, P., et al. Didehydro-cortistatin A inhibits HIV-1 by specifically binding to the unstructured basic region of Tat MBio  2019 10:e02662-18  DOI:10.1128/mBio.02662-18  PMID:30723126  PMCID:PMC6368365
    • Patil, D. N., Rangarajan, E. S., Novick, S. J., Pascal, B. D., Kojetin, D. J., Griffin, P. R., Izard, T., Martemyanov, K. A. Structural organization of a major neuronal G protein regulator, the RGS7-Gβ5-R7BP complex Elife  2018 7  DOI:10.7554/eLife.42150  PMID:30540250  PMCID:PMC6310461
    • Chinthalapudi, K., Rangarajan, E. S., Izard, T. The interaction of talin with the cell membrane is essential for integrin activation and focal adhesion formation Proceedings of the National Academy of Sciences of the United States of America  2018 115:10339-10344  DOI:10.1073/pnas.1806275115  PMID:30254158  PMCID:PMC6187153
    • Chinthalapudi, K., Mandati, V., Zheng, J., Sharff, A. J., Bricogne, G., Griffin, P. R., Kissil, J., Izard, T. Lipid binding promotes the open conformation and tumor-suppressive activity of neurofibromin 2 Nature Communications  2018 9  DOI:10.1038/s41467-018-03648-4  PMID:29626191  PMCID:PMC5889391
    • Cao, W., Kayama, H., Chen, M. L., Delmas, A., Sun, A., Kim, S. Y., Rangarajan, E. S., McKevitt, K., Beck, A. P., Jackson, C. B., Crynen, G., Oikonomopoulos, A., et al. The Xenobiotic Transporter Mdr1 Enforces T Cell Homeostasis in the Presence of Intestinal Bile Acids Immunity  2017 47:1182-1196  DOI:10.1016/j.immuni.2017.11.012  PMID:29262351  PMCID:PMC5741099
    • Stender, J. D., Nwachukwu, J. C., Kastrati, I., Kim, Y., Strid, T., Yakir, M., Srinivasan, S., Nowak, J., Izard, T., Rangarajan, E. S., Carlson, K. E., Katzenellenbogen, J. A., et al. Structural and molecular mechanisms of cytokine-mediated endocrine resistance in human breast cancer cells Molecular Cell  2017 65:1122-1135  DOI:10.1016/j.molcel.2017.02.008  PMID:28306507
    • Nwachukwu, J. C., Srinivasan, S., Bruno, N. E., Nowak, J., Wright, N. J., Minutolo, F., Rangarajan, E. S., Izard, T., Yao, X. Q., Grant, B. J., Kojetin, D. J., Elemento, O., et al. Systems structural biology analysis of ligand effects on ERα predicts cellular response to environmental estrogens and anti-hormone therapies Cell Chemical Biology  2017 24:35-45  DOI:10.1016/j.chembiol.2016.11.014  PMID:28042045
    • Chinthalapudi, K., Rangarajan, E. S., Brown, D. T., Izard, T. Differential lipid binding of vinculin isoforms promotes quasi-equivalent dimerization Proceedings of the National Academy of Sciences of the United States of America  2016 113:9539-9544  DOI:10.1073/pnas.1600702113  PMID:27503891  PMCID:PMC5003255
    • Izard, T., Brown, D. T. Mechanisms and functions of vinculin interactions with phospholipids at cell adhesion sites Journal of Biological Chemistry  2016 291:2548-2555  DOI:10.1074/jbc.R115.686493  PMID:26728462  PMCID:PMC4742724
    • Brown, D. T., Izard, T. Vinculin-cell membrane interactions Oncotarget  2015 6:34043-34044  DOI:10.18632/oncotarget.5868  PMID:26431280  PMCID:PMC4741423
    • Chinthalapudi, K., Patil, D. N., Rangarajan, E. S., Rader, C., Izard, T. Lipid-directed vinculin dimerization Biochemistry  2015 54:2758-2768  DOI:10.1021/acs.biochem.5b00015  PMID:25880222
    • Chinthalapudi, K., Rangarajan, E. S., Patil, D. N., George, E. M., Brown, D. T., Izard, T. Lipid binding promotes oligomerization and focal adhesion activity of vinculin Journal of Cell Biology  2014 207:643-656  DOI:10.1083/jcb.201404128  PMID:25488920  PMCID:PMC4259812
    • Poussin, K., Pilati, C., Couchy, G., Calderaro, J., Bioulac-Sage, P., Bacq, Y., Paradis, V., Leteurtre, E., Sturm, N., Ramos, J., Guettier, C., Bardier-Dupas, A., et al. Biochemical and functional analyses of gp130 mutants unveil JAK1 as a novel therapeutic target in human inflammatory hepatocellular adenoma Oncoimmunology  2013 2:e27090  DOI:10.4161/onci.27090  PMID:24501689  PMCID:PMC3913689
    • Lee, J. H., Vonrhein, C., Bricogne, G., Izard, T. Crystal structure of the N-terminal domains of the surface cell antigen 4 of Rickettsia Protein Science  2013 22:1425-1431  DOI:10.1002/pro.2322  PMID:23904352  PMCID:PMC3795500
    • Rangarajan, E. S., Izard, T. Dimer asymmetry defines α-catenin interactions Nature Structural & Molecular Biology  2013 20:188-193  DOI:10.1038/nsmb.2479  PMID:23292143  PMCID:PMC3805043
    • Rangarajan, E. S., Izard, T. The Cytoskeletal Protein α-Catenin unfurls upon binding to vinculin Journal of Biological Chemistry  2012 287:18492-18499  DOI:10.1074/jbc.M112.351023  PMID:22493458  PMCID:PMC3365723
    • Yogesha, S. D., Rangarajan, E. S., Vonrhein, C., Bricogne, G., Izard, T. Crystal structure of vinculin in complex with vinculin binding site 50 (VBS50), the integrin binding site 2 (IBS2) of talin Protein Science  2012 21:583-588  DOI:10.1002/pro.2041  PMID:22334306  PMCID:PMC3375758
    • Lee, J. H., Rangarajan, E. S., Vonrhein, C., Bricogne, G., Izard, T. The metavinculin tail domain directs constitutive interactions with raver1 and vinculin RNA Journal of Molecular Biology  2012 422:697-704  DOI:10.1016/j.jmb.2012.06.015  PMID:22709580  PMCID:PMC3835166
    • Yogesha, S. D., Sharff, A. J., Giovannini, M., Bricogne, G., Izard, T. Unfurling of the band 4.1, ezrin, radixin, moesin (FERM) domain of the merlin tumor suppressor Protein Science  2011 20:2113-2120  DOI:10.1002/pro.751  PMID:22012890  PMCID:PMC3302654
    • Park, H., Lee, J. H., Gouin, E., Cossart, P., Izard, T. The rickettsia surface cell antigen 4 applies mimicry to bind to and activate vinculin Journal of Biological Chemistry  2011 286:35096-35103  DOI:10.1074/jbc.M111.263855  PMID:21841197  PMCID:PMC3186400
    • Rangarajan, E. S., Lee, J. H., Izard, T. Apo raver1 structure reveals distinct RRM domain orientations Protein Science  2011 20:1464-1470  DOI:10.1002/pro.664  PMID:21633983  PMCID:PMC3189531
    • Yogesha, S. D., Sharff, A., Bricogne, G., Izard, T. Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin Protein Science  2011 20:1471-1476  DOI:10.1002/pro.671  PMID:21648001  PMCID:PMC3189532
    • Pilati, C., Amessou, M., Bihl, M. P., Balabaud, C., Jeanne, T. V. N., Paradis, V., Nault, J. C., Izard, T., Bioulac-Sage, P., Couchy, G., Poussin, K., Zucman-Rossi, J. Somatic mutations activating STAT3 in human inflammatory hepatocellular adenomas Journal of Experimental Medicine  2011 208:1359-1366  DOI:10.1084/jem.20110283  PMID:21690253  PMCID:PMC3135371
    • Park, H., Valencia-Gallardo, C., Sharff, A., Guy, T. V. N., Izard, T. Novel vinculin binding site of the IpaA invasin of Shigella Journal of Biological Chemistry  2011 286:23214-23221  DOI:10.1074/jbc.M110.184283  PMID:21525010  PMCID:PMC3123088
    • Rangarajan, E. S., Izard, T. Improving the diffraction of full-length human selenomethionyl metavinculin crystals by streak-seeding Acta Crystallographica Section F-Structural Biology and Crystallization Communications  2010 66:1617-1620  DOI:10.1107/s1744309110041059  PMID:21139209  PMCID:PMC2998368
    • George, E. M., Izard, T., Anderson, S. D., Brown, D. T. Nucleosome interaction surface of linker histone H1c is distinct from that of H1(0) Journal of Biological Chemistry  2010 285:20891-20896  DOI:10.1074/jbc.M110.108639  PMID:20444700  PMCID:PMC2898364
    • Rangarajan, E. S., Lee, J. H., Yogesha, S. D., Izard, T. A helix replacement mechanism directs metavinculin functions PLoS One  2010 5:e10679  DOI:10.1371/journal.pone.0010679  PMID:20502710  PMCID:PMC2873289
    • Park, H., Rangarajan, E. S., Sygusch, J., Izard, T. Dramatic improvement of crystal quality for low-temperature-grown rabbit muscle aldolase Acta Crystallographica Section F-Structural Biology and Crystallization Communications  2010 66:595-600  DOI:10.1107/s1744309110011875  PMID:20445268  PMCID:PMC2864701
    • Rangarajan, E. S., Park, H., Fortin, E., Sygusch, J., Izard, T. Mechanism of aldolase control of sorting nexin 9 function in endocytosis Journal of Biological Chemistry  2010 285:11983-11990  DOI:10.1074/jbc.M109.092049  PMID:20129922  PMCID:PMC2852936
    • Lee, J. H., Rangarajan, E. S., Yogesha, S. D., Izard, T. Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions Structure  2009 17:833-842  DOI:10.1016/j.str.2009.04.010  PMID:19523901  PMCID:PMC2811071
    • Rebouissou, S., Amessou, M., Couchy, G., Poussin, K., Imbeaud, S., Pilati, C., Izard, T., Balabaud, C., Bioulac-Sage, P., Zucman-Rossi, J. Frequent in-frame somatic deletions activate gp130 in inflammatory hepatocellular tumours Nature  2009 457:200-204  DOI:10.1038/nature07475  PMID:19020503  PMCID:PMC2695248
    • Van Nhieu, G. T., Izard, T. Vinculin binding in its closed conformation by a helix addition mechanism EMBO Journal  2007 26:4588-4596  DOI:10.1038/sj.emboj.7601863  PMID:17932491  PMCID:PMC2063484
    • St-Jean, M., Izard, T., Sygusch, J. A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein Journal of Biological Chemistry  2007 282:14309-14315  DOI:10.1074/jbc.M611505200  PMID:17329259
    • Ramarao, N., Le Clainche, C., Izard, T., Bourdet-Sicard, R., Ageron, E., Sansonetti, P. J., Carlier, M. F., Van Nhieu, G. T. Capping of actin filaments by vinculin activated by the Shigella IpaA carboxyl-terminal domain FEBS Letters  2007 581:853-857  DOI:10.1016/j.febslet.2007.01.057  PMID:17289036
    • Izard, T., Van Nhieu, G. T., Bois, P. R. J. Shigella applies molecular mimicry to subvert vinculin and invade host cells Journal of Cell Biology  2006 175:465-475  DOI:10.1083/jcb.200605091  PMID:17088427  PMCID:PMC2064523
    • Bois, P. R. J., O'Hara, B. P., Nietlispach, D., Kirkpatrick, J., Izard, T. The vinculin binding sites of talin and alpha-actinin are sufficient to activate vinculin Journal of Biological Chemistry  2006 281:7228-7236  DOI:10.1074/jbc.M510397200  PMID:16407299
    • Brown, D. T., Izard, T., Misteli, T. Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo Nature Structural & Molecular Biology  2006 13:250-255  DOI:10.1038/nsmb1050  PMID:16462749  PMCID:PMC1868459
    • Bois, P. R. J., Borgon, R. A., Vonrhein, C., Izard, T. Structural dynamics of alpha-actinin-vinculin interactions Molecular and Cellular Biology  2005 25:6112-6122  DOI:10.1128/mcb.25.14.6112-6122.2005  PMID:15988023
    • Morris, V. K., Izard, T. Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase Protein Science  2004 13:2547-2552  DOI:10.1110/ps.04816904  PMID:15322293  PMCID:PMC2280004
    • Borgon, R. A., Vonrhein, C., Bricogne, G., Bois, P. R. J., Izard, T. Crystal structure of human vinculin Structure  2004 12:1189-1197  DOI:10.1016/j.str.2004.05.009  PMID:15242595
    • Izard, T., Vonrhein, C. Structural basis for amplifying vinculin activation by talin Journal of Biological Chemistry  2004 279:27667-27678  DOI:10.1074/jbc.M403076200  PMID:15070891
    • Rush, C. L., Izard, T. Rhombohedral crystals of the human vinculin head domain in complex with a vinculin-binding site of talin Acta Crystallographica Section D-Biological Crystallography  2004 60:945-947  DOI:10.1107/s0907444904006547  PMID:15103147
    • Izard, T., Evans, G., Borgon, R. A., Rush, C. L., Bricogne, G., Bois, P. R. J. Vinculin activation by talin through helical bundle conversion Nature  2004 427:171-175  DOI:10.1038/nature02281  PMID:14702644
    • Izard, T., Sygusch, J. Induced fit movements and metal cofactor selectivity of class ll aldolases - structure of Thermus aquaticus fructose-1,6-bisphosphate aldolase Journal of Biological Chemistry  2004 279:11825-11833  DOI:10.1074/jbc.M311375200  PMID:14699122
    • Brown, K. L., Morris, V. K., Izard, T. Rhombohedral crystals of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase Acta Crystallographica Section D-Biological Crystallography  2004 60:195-196  DOI:10.1107/s0907444903025988  PMID:14684928
    • Izard, T. A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A Journal of Bacteriology  2003 185:4074-4080  DOI:10.1128/jb.185.14.4074-4080.2003  PMID:12837781
    • Hurlbert, J. C., Izard, T. Crystallization of HLA-DR4 fused to an immunodominant collagen ll peptide implicated in rheumatoid arthritis Acta Crystallographica Section D-Biological Crystallography  2002 58:1749-1751  DOI:10.1107/s0907444902014142  PMID:12351899
    • Izard, T. The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism Journal of Molecular Biology  2002 315:487-495  DOI:10.1006/jmbi.2001.5272  PMID:11812124
    • Izard, T. Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity Protein Science  2001 10:1508-1513  DOI:10.1110/ps.10.8.1508  PMID:11468347
    • Izard, T., Blackwell, N. C. Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism EMBO Journal  2000 19:3849-3856  DOI:10.1093/emboj/19.15.3849  PMID:10921867  PMCID:PMC306599
    • Izard, T., Ellis, J. The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism EMBO Journal  2000 19:2690-2700  DOI:10.1093/emboj/19.11.2690  PMID:10835366  PMCID:PMC212772
    • Blackwell, N. C., Cullis, P. M., Cooper, R. A., Izard, T. Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli Acta Crystallographica Section D-Biological Crystallography  1999 55:1368-1369  DOI:10.1107/s0907444999006502  PMID:10393309
    • Izard, T., Geerlof, A., Lewendon, A., Barker, J. J. Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli Acta Crystallographica Section D-Biological Crystallography  1999 55:1226-1228  DOI:10.1107/s0907444999004394  PMID:10329792
    • Ellis, J., Campopiano, D. J., Izard, T. Cubic crystals of chloramphenicol phosphotransferase from Streptomyces venezuelae in complex with chloramphenicol Acta Crystallographica Section D-Biological Crystallography  1999 55:1086-1088  DOI:10.1107/s0907444999003029  PMID:10216290
    • Izard, T., Geerlof, A. The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity EMBO Journal  1999 18:2021-2030  DOI:10.1093/emboj/18.8.2021  PMID:10205156  PMCID:PMC1171286
    • Izard, T., Aevarsson, A., Allen, M. D., Westphal, A. H., Perham, R. N., de Kok, A., Hol, W. G. J. Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes Proceedings of the National Academy of Sciences of the United States of America  1999 96:1240-1245  DOI:10.1073/pnas.96.4.1240  PMID:9990008
    • Izard, T., Sarfaty, S., Westphal, A., DeKok, A., Hol, W. G. J. Improvement of diffraction quality upon rehydration of dehydrated icosahedral Enterococcus faecalis pyruvate dehydrogenase core crystals Protein Science  1997 6:913-915  DOI:10.1002/pro.5560060419  PMID:9098902  PMCID:PMC2144755
    • Lawrence, M. C., Izard, T., Beuchat, M., Blagrove, R. J., Colman, P. M. Structure of phaseolin at 2.2 Å resolution - implications for a common vicilin/legumin structure and the genetic-engineering of seed storage proteins Journal of Molecular Biology  1994 238:748-776  DOI:10.1006/jmbi.1994.1333  PMID:8182747
    • Izard, T., Lawrence, M. C., Malby, R. L., Lilley, G. G., Colman, P. M. The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli Structure  1994 2:361-369  DOI:10.1016/s0969-2126(00)00038-1  PMID:8081752
    • Izard, T., Fol, B., Pauptit, R. A., Jansonius, J. N. Trigonal crystals of porcine mitochondrial aspartate-aminotransferase Journal of Molecular Biology  1990 215:341-344  DOI:10.1016/s0022-2836(05)80355-9  PMID:2231709
  • thesis

    • Three dimensional Fourier synthesis of N-acetylneuraminate lyase from Escherichia coli

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Research

research overview

  • Cell migration and morphogenesis relies on the cell?s ability to form specific contacts with its neighbors (adherens junctions) or with the extracellular matrix (focal adhesions). Focal adhesions are directed by integrin receptors, which are unique in provoking both outside-in and inside-out signaling pathways. Integrin receptor activation triggers the rapid reorganization of the actin cytoskeleton and this relies on the function of talin and vinculin, which were thought to simply act as scaffolds that bridge integrin receptors to the actin cytoskeleton. We have taken structural, biochemical, and biological approaches to determine the roles of talin and vinculin. Surprisingly, our studies have revealed that these proteins function as direct signaling effectors that, by undergoing dramatic changes in their structures, transmit the outside-in signal.
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Background

education and training

  • Ph.D., The University of Melbourne 1994
  • M.S., University of Basel 1990
  • B.S., University of Basel 1988
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Contact

full name

  • T. Izard Bois

geographic location

  • Scripps Florida 
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Identity

ORCID iD

  • ORCID iD http://orcid.org/0000-0002-2895-483x

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