[{"ddc":["570"],"month":"08","date_created":"2018-12-12T12:31:34Z","has_accepted_license":"1","keyword":["Immunological synapse"],"oa":1,"datarep_id":"71","type":"research_data","tmp":{"short":"CC0 (1.0)","legal_code_url":"https://creativecommons.org/publicdomain/zero/1.0/legalcode","image":"/images/cc_0.png","name":"Creative Commons Public Domain Dedication (CC0 1.0)"},"citation":{"mla":"Leithner, Alexander F. <i>Immunological Synapse DC-Tcells</i>. Institute of Science and Technology Austria, 2017, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:71\">10.15479/AT:ISTA:71</a>.","ama":"Leithner AF. Immunological synapse DC-Tcells. 2017. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:71\">10.15479/AT:ISTA:71</a>","ista":"Leithner AF. 2017. Immunological synapse DC-Tcells, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT:ISTA:71\">10.15479/AT:ISTA:71</a>.","short":"A.F. Leithner, (2017).","chicago":"Leithner, Alexander F. “Immunological Synapse DC-Tcells.” Institute of Science and Technology Austria, 2017. <a href=\"https://doi.org/10.15479/AT:ISTA:71\">https://doi.org/10.15479/AT:ISTA:71</a>.","ieee":"A. F. Leithner, “Immunological synapse DC-Tcells.” Institute of Science and Technology Austria, 2017.","apa":"Leithner, A. F. (2017). Immunological synapse DC-Tcells. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:71\">https://doi.org/10.15479/AT:ISTA:71</a>"},"author":[{"orcid":"0000-0002-1073-744X","id":"3B1B77E4-F248-11E8-B48F-1D18A9856A87","first_name":"Alexander F","last_name":"Leithner","full_name":"Leithner, Alexander F"}],"_id":"5567","date_updated":"2024-02-21T13:47:00Z","article_processing_charge":"No","publisher":"Institute of Science and Technology Austria","year":"2017","oa_version":"Published Version","day":"09","date_published":"2017-08-09T00:00:00Z","department":[{"_id":"MiSi"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","doi":"10.15479/AT:ISTA:71","file_date_updated":"2020-07-14T12:47:04Z","license":"https://creativecommons.org/publicdomain/zero/1.0/","file":[{"date_updated":"2020-07-14T12:47:04Z","access_level":"open_access","file_size":236204020,"date_created":"2018-12-12T13:02:47Z","creator":"system","content_type":"video/x-msvideo","checksum":"3d6942d47d0737d064706b5728c4d8c8","file_name":"IST-2017-71-v1+1_Synapse_1.avi","relation":"main_file","file_id":"5612"},{"relation":"main_file","file_id":"5613","creator":"system","file_name":"IST-2017-71-v1+2_Synapse_2.avi","content_type":"video/x-msvideo","checksum":"4850006c047b0147a9e85b3c2f6f0af4","date_created":"2018-12-12T13:02:51Z","file_size":226232496,"date_updated":"2020-07-14T12:47:04Z","access_level":"open_access"}],"title":"Immunological synapse DC-Tcells","status":"public","abstract":[{"lang":"eng","text":"Immunological synapse DC-Tcells"}]},{"doi":"10.7554/eLife.30867","external_id":{"isi":["000414407700001"]},"title":"Cytokinesis in vertebrate cells initiates by contraction of an equatorial actomyosin network composed of randomly oriented filaments","abstract":[{"lang":"eng","text":"The actomyosin ring generates force to ingress the cytokinetic cleavage furrow in animal cells, yet its filament organization and the mechanism of contractility is not well understood. We quantified actin filament order in human cells using fluorescence polarization microscopy and found that cleavage furrow ingression initiates by contraction of an equatorial actin network with randomly oriented filaments. The network subsequently gradually reoriented actin filaments along the cell equator. This strictly depended on myosin II activity, suggesting local network reorganization by mechanical forces. Cortical laser microsurgery revealed that during cytokinesis progression, mechanical tension increased substantially along the direction of the cell equator, while the network contracted laterally along the pole-to-pole axis without a detectable increase in tension. Our data suggest that an asymmetric increase in cortical tension promotes filament reorientation along the cytokinetic cleavage furrow, which might have implications for diverse other biological processes involving actomyosin rings."}],"date_updated":"2025-09-11T07:41:10Z","publication_status":"published","scopus_import":"1","language":[{"iso":"eng"}],"oa_version":"Published Version","oa":1,"intvolume":"         6","month":"11","isi":1,"ddc":["570"],"date_created":"2018-12-11T11:47:14Z","publication":"eLife","publist_id":"7245","file_date_updated":"2020-07-14T12:47:10Z","volume":6,"status":"public","license":"https://creativecommons.org/licenses/by/4.0/","file":[{"file_size":9666973,"date_created":"2018-12-12T10:10:40Z","access_level":"open_access","date_updated":"2020-07-14T12:47:10Z","file_id":"4829","relation":"main_file","file_name":"IST-2017-919-v1+1_elife-30867-figures-v1.pdf","checksum":"ba09c1451153d39e4f4b7cee013e314c","content_type":"application/pdf","creator":"system"},{"access_level":"open_access","date_updated":"2020-07-14T12:47:10Z","file_size":5951246,"date_created":"2018-12-12T10:10:41Z","checksum":"01eb51f1d6ad679947415a51c988e137","content_type":"application/pdf","file_name":"IST-2017-919-v1+2_elife-30867-v1.pdf","creator":"system","file_id":"4830","relation":"main_file"}],"author":[{"last_name":"Spira","full_name":"Spira, Felix","first_name":"Felix"},{"first_name":"Sara","full_name":"Cuylen Haering, Sara","last_name":"Cuylen Haering"},{"first_name":"Shalin","full_name":"Mehta, Shalin","last_name":"Mehta"},{"last_name":"Samwer","full_name":"Samwer, Matthias","first_name":"Matthias"},{"orcid":"0000-0003-0666-8928","first_name":"Anne","id":"35B76592-F248-11E8-B48F-1D18A9856A87","last_name":"Reversat","full_name":"Reversat, Anne"},{"last_name":"Verma","full_name":"Verma, Amitabh","first_name":"Amitabh"},{"first_name":"Rudolf","full_name":"Oldenbourg, Rudolf","last_name":"Oldenbourg"},{"orcid":"0000-0002-6620-9179","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K","last_name":"Sixt","full_name":"Sixt, Michael K"},{"last_name":"Gerlich","full_name":"Gerlich, Daniel","first_name":"Daniel"}],"_id":"569","article_processing_charge":"No","publisher":"eLife Sciences Publications","pubrep_id":"919","date_published":"2017-11-06T00:00:00Z","day":"06","year":"2017","department":[{"_id":"MiSi"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","quality_controlled":"1","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"citation":{"ieee":"F. Spira <i>et al.</i>, “Cytokinesis in vertebrate cells initiates by contraction of an equatorial actomyosin network composed of randomly oriented filaments,” <i>eLife</i>, vol. 6. eLife Sciences Publications, 2017.","apa":"Spira, F., Cuylen Haering, S., Mehta, S., Samwer, M., Reversat, A., Verma, A., … Gerlich, D. (2017). Cytokinesis in vertebrate cells initiates by contraction of an equatorial actomyosin network composed of randomly oriented filaments. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/eLife.30867\">https://doi.org/10.7554/eLife.30867</a>","short":"F. Spira, S. Cuylen Haering, S. Mehta, M. Samwer, A. Reversat, A. Verma, R. Oldenbourg, M.K. Sixt, D. Gerlich, ELife 6 (2017).","chicago":"Spira, Felix, Sara Cuylen Haering, Shalin Mehta, Matthias Samwer, Anne Reversat, Amitabh Verma, Rudolf Oldenbourg, Michael K Sixt, and Daniel Gerlich. “Cytokinesis in Vertebrate Cells Initiates by Contraction of an Equatorial Actomyosin Network Composed of Randomly Oriented Filaments.” <i>ELife</i>. eLife Sciences Publications, 2017. <a href=\"https://doi.org/10.7554/eLife.30867\">https://doi.org/10.7554/eLife.30867</a>.","ista":"Spira F, Cuylen Haering S, Mehta S, Samwer M, Reversat A, Verma A, Oldenbourg R, Sixt MK, Gerlich D. 2017. Cytokinesis in vertebrate cells initiates by contraction of an equatorial actomyosin network composed of randomly oriented filaments. eLife. 6, e30867.","ama":"Spira F, Cuylen Haering S, Mehta S, et al. Cytokinesis in vertebrate cells initiates by contraction of an equatorial actomyosin network composed of randomly oriented filaments. <i>eLife</i>. 2017;6. doi:<a href=\"https://doi.org/10.7554/eLife.30867\">10.7554/eLife.30867</a>","mla":"Spira, Felix, et al. “Cytokinesis in Vertebrate Cells Initiates by Contraction of an Equatorial Actomyosin Network Composed of Randomly Oriented Filaments.” <i>ELife</i>, vol. 6, e30867, eLife Sciences Publications, 2017, doi:<a href=\"https://doi.org/10.7554/eLife.30867\">10.7554/eLife.30867</a>."},"article_number":"e30867","has_accepted_license":"1","publication_identifier":{"issn":["2050-084X"]}},{"project":[{"_id":"260AA4E2-B435-11E9-9278-68D0E5697425","name":"Mechanical Adaptation of Lamellipodial Actin Networks in Migrating Cells","call_identifier":"H2020","grant_number":"747687"}],"quality_controlled":"1","type":"journal_article","citation":{"mla":"Gärtner, Florian R., et al. “Migrating Platelets Are Mechano Scavengers That Collect and Bundle Bacteria.” <i>Cell Press</i>, vol. 171, no. 6, Cell Press, 2017, pp. 1368–82, doi:<a href=\"https://doi.org/10.1016/j.cell.2017.11.001\">10.1016/j.cell.2017.11.001</a>.","ista":"Gärtner FR, Ahmad Z, Rosenberger G, Fan S, Nicolai L, Busch B, Yavuz G, Luckner M, Ishikawa Ankerhold H, Hennel R, Benechet A, Lorenz M, Chandraratne S, Schubert I, Helmer S, Striednig B, Stark K, Janko M, Böttcher R, Verschoor A, Leon C, Gachet C, Gudermann T, Mederos Y Schnitzler M, Pincus Z, Iannacone M, Haas R, Wanner G, Lauber K, Sixt MK, Massberg S. 2017. Migrating platelets are mechano scavengers that collect and bundle bacteria. Cell Press. 171(6), 1368–1382.","ama":"Gärtner FR, Ahmad Z, Rosenberger G, et al. Migrating platelets are mechano scavengers that collect and bundle bacteria. <i>Cell Press</i>. 2017;171(6):1368-1382. doi:<a href=\"https://doi.org/10.1016/j.cell.2017.11.001\">10.1016/j.cell.2017.11.001</a>","short":"F.R. Gärtner, Z. Ahmad, G. Rosenberger, S. Fan, L. Nicolai, B. Busch, G. Yavuz, M. Luckner, H. Ishikawa Ankerhold, R. Hennel, A. Benechet, M. Lorenz, S. Chandraratne, I. Schubert, S. Helmer, B. Striednig, K. Stark, M. Janko, R. Böttcher, A. Verschoor, C. Leon, C. Gachet, T. Gudermann, M. Mederos Y Schnitzler, Z. Pincus, M. Iannacone, R. Haas, G. Wanner, K. Lauber, M.K. Sixt, S. Massberg, Cell Press 171 (2017) 1368–1382.","chicago":"Gärtner, Florian R, Zerkah Ahmad, Gerhild Rosenberger, Shuxia Fan, Leo Nicolai, Benjamin Busch, Gökce Yavuz, et al. “Migrating Platelets Are Mechano Scavengers That Collect and Bundle Bacteria.” <i>Cell Press</i>. Cell Press, 2017. <a href=\"https://doi.org/10.1016/j.cell.2017.11.001\">https://doi.org/10.1016/j.cell.2017.11.001</a>.","ieee":"F. R. Gärtner <i>et al.</i>, “Migrating platelets are mechano scavengers that collect and bundle bacteria,” <i>Cell Press</i>, vol. 171, no. 6. Cell Press, pp. 1368–1382, 2017.","apa":"Gärtner, F. R., Ahmad, Z., Rosenberger, G., Fan, S., Nicolai, L., Busch, B., … Massberg, S. (2017). Migrating platelets are mechano scavengers that collect and bundle bacteria. <i>Cell Press</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.cell.2017.11.001\">https://doi.org/10.1016/j.cell.2017.11.001</a>"},"issue":"6","publication_identifier":{"issn":["0092-8674"]},"publist_id":"7243","volume":171,"ec_funded":1,"status":"public","author":[{"full_name":"Gärtner, Florian R","last_name":"Gärtner","id":"397A88EE-F248-11E8-B48F-1D18A9856A87","first_name":"Florian R","orcid":"0000-0001-6120-3723"},{"first_name":"Zerkah","full_name":"Ahmad, Zerkah","last_name":"Ahmad"},{"first_name":"Gerhild","last_name":"Rosenberger","full_name":"Rosenberger, Gerhild"},{"last_name":"Fan","full_name":"Fan, Shuxia","first_name":"Shuxia"},{"first_name":"Leo","full_name":"Nicolai, Leo","last_name":"Nicolai"},{"first_name":"Benjamin","full_name":"Busch, Benjamin","last_name":"Busch"},{"first_name":"Gökce","last_name":"Yavuz","full_name":"Yavuz, Gökce"},{"last_name":"Luckner","full_name":"Luckner, Manja","first_name":"Manja"},{"last_name":"Ishikawa Ankerhold","full_name":"Ishikawa Ankerhold, Hellen","first_name":"Hellen"},{"last_name":"Hennel","full_name":"Hennel, Roman","first_name":"Roman"},{"first_name":"Alexandre","last_name":"Benechet","full_name":"Benechet, Alexandre"},{"first_name":"Michael","last_name":"Lorenz","full_name":"Lorenz, Michael"},{"first_name":"Sue","last_name":"Chandraratne","full_name":"Chandraratne, Sue"},{"first_name":"Irene","full_name":"Schubert, Irene","last_name":"Schubert"},{"full_name":"Helmer, Sebastian","last_name":"Helmer","first_name":"Sebastian"},{"first_name":"Bianca","full_name":"Striednig, Bianca","last_name":"Striednig"},{"first_name":"Konstantin","full_name":"Stark, Konstantin","last_name":"Stark"},{"first_name":"Marek","full_name":"Janko, Marek","last_name":"Janko"},{"last_name":"Böttcher","full_name":"Böttcher, Ralph","first_name":"Ralph"},{"first_name":"Admar","full_name":"Verschoor, Admar","last_name":"Verschoor"},{"full_name":"Leon, Catherine","last_name":"Leon","first_name":"Catherine"},{"last_name":"Gachet","full_name":"Gachet, Christian","first_name":"Christian"},{"first_name":"Thomas","full_name":"Gudermann, Thomas","last_name":"Gudermann"},{"first_name":"Michael","last_name":"Mederos Y Schnitzler","full_name":"Mederos Y Schnitzler, Michael"},{"first_name":"Zachary","full_name":"Pincus, Zachary","last_name":"Pincus"},{"full_name":"Iannacone, Matteo","last_name":"Iannacone","first_name":"Matteo"},{"first_name":"Rainer","last_name":"Haas","full_name":"Haas, Rainer"},{"last_name":"Wanner","full_name":"Wanner, Gerhard","first_name":"Gerhard"},{"first_name":"Kirsten","last_name":"Lauber","full_name":"Lauber, Kirsten"},{"orcid":"0000-0002-6620-9179","first_name":"Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","last_name":"Sixt","full_name":"Sixt, Michael K"},{"first_name":"Steffen","last_name":"Massberg","full_name":"Massberg, Steffen"}],"_id":"571","article_processing_charge":"No","publisher":"Cell Press","date_published":"2017-11-30T00:00:00Z","year":"2017","day":"30","department":[{"_id":"MiSi"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","intvolume":"       171","month":"11","isi":1,"date_created":"2018-12-11T11:47:15Z","page":"1368 - 1382","publication":"Cell Press","doi":"10.1016/j.cell.2017.11.001","external_id":{"isi":["000417362700018"]},"title":"Migrating platelets are mechano scavengers that collect and bundle bacteria","abstract":[{"text":"Blood platelets are critical for hemostasis and thrombosis and play diverse roles during immune responses. Despite these versatile tasks in mammalian biology, their skills on a cellular level are deemed limited, mainly consisting in rolling, adhesion, and aggregate formation. Here, we identify an unappreciated asset of platelets and show that adherent platelets use adhesion receptors to mechanically probe the adhesive substrate in their local microenvironment. When actomyosin-dependent traction forces overcome substrate resistance, platelets migrate and pile up the adhesive substrate together with any bound particulate material. They use this ability to act as cellular scavengers, scanning the vascular surface for potential invaders and collecting deposited bacteria. Microbe collection by migrating platelets boosts the activity of professional phagocytes, exacerbating inflammatory tissue injury in sepsis. This assigns platelets a central role in innate immune responses and identifies them as potential targets to dampen inflammatory tissue damage in clinical scenarios of severe systemic infection. In addition to their role in thrombosis and hemostasis, platelets can also migrate to sites of infection to help trap bacteria and clear the vascular surface.","lang":"eng"}],"publication_status":"published","date_updated":"2025-09-11T07:39:45Z","scopus_import":"1","language":[{"iso":"eng"}],"oa_version":"None"},{"month":"03","isi":1,"ddc":["570"],"date_created":"2018-12-11T11:47:46Z","publication":"Nature Communications","oa":1,"intvolume":"         8","scopus_import":"1","publication_status":"published","date_updated":"2025-09-11T07:09:28Z","language":[{"iso":"eng"}],"oa_version":"Published Version","doi":"10.1038/ncomms14832","title":"FMNL formins boost lamellipodial force generation","abstract":[{"text":"Migration frequently involves Rac-mediated protrusion of lamellipodia, formed by Arp2/3 complex-dependent branching thought to be crucial for force generation and stability of these networks. The formins FMNL2 and FMNL3 are Cdc42 effectors targeting to the lamellipodium tip and shown here to nucleate and elongate actin filaments with complementary activities in vitro. In migrating B16-F1 melanoma cells, both formins contribute to the velocity of lamellipodium protrusion. Loss of FMNL2/3 function in melanoma cells and fibroblasts reduces lamellipodial width, actin filament density and -bundling, without changing patterns of Arp2/3 complex incorporation. Strikingly, in melanoma cells, FMNL2/3 gene inactivation almost completely abolishes protrusion forces exerted by lamellipodia and modifies their ultrastructural organization. Consistently, CRISPR/Cas-mediated depletion of FMNL2/3 in fibroblasts reduces both migration and capability of cells to move against viscous media. Together, we conclude that force generation in lamellipodia strongly depends on FMNL formin activity, operating in addition to Arp2/3 complex-dependent filament branching.","lang":"eng"}],"external_id":{"isi":["000396993700001"]},"article_number":"14832","has_accepted_license":"1","publication_identifier":{"issn":["2041-1723"]},"quality_controlled":"1","type":"journal_article","citation":{"mla":"Kage, Frieda, et al. “FMNL Formins Boost Lamellipodial Force Generation.” <i>Nature Communications</i>, vol. 8, 14832, Nature Publishing Group, 2017, doi:<a href=\"https://doi.org/10.1038/ncomms14832\">10.1038/ncomms14832</a>.","ista":"Kage F, Winterhoff M, Dimchev V, Müller J, Thalheim T, Freise A, Brühmann S, Kollasser J, Block J, Dimchev GA, Geyer M, Schnittler H, Brakebusch C, Stradal T, Carlier M, Sixt MK, Käs J, Faix J, Rottner K. 2017. FMNL formins boost lamellipodial force generation. Nature Communications. 8, 14832.","ama":"Kage F, Winterhoff M, Dimchev V, et al. FMNL formins boost lamellipodial force generation. <i>Nature Communications</i>. 2017;8. doi:<a href=\"https://doi.org/10.1038/ncomms14832\">10.1038/ncomms14832</a>","apa":"Kage, F., Winterhoff, M., Dimchev, V., Müller, J., Thalheim, T., Freise, A., … Rottner, K. (2017). FMNL formins boost lamellipodial force generation. <i>Nature Communications</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/ncomms14832\">https://doi.org/10.1038/ncomms14832</a>","ieee":"F. Kage <i>et al.</i>, “FMNL formins boost lamellipodial force generation,” <i>Nature Communications</i>, vol. 8. Nature Publishing Group, 2017.","chicago":"Kage, Frieda, Moritz Winterhoff, Vanessa Dimchev, Jan Müller, Tobias Thalheim, Anika Freise, Stefan Brühmann, et al. “FMNL Formins Boost Lamellipodial Force Generation.” <i>Nature Communications</i>. Nature Publishing Group, 2017. <a href=\"https://doi.org/10.1038/ncomms14832\">https://doi.org/10.1038/ncomms14832</a>.","short":"F. Kage, M. Winterhoff, V. Dimchev, J. Müller, T. Thalheim, A. Freise, S. Brühmann, J. Kollasser, J. Block, G.A. Dimchev, M. Geyer, H. Schnittler, C. Brakebusch, T. Stradal, M. Carlier, M.K. Sixt, J. Käs, J. Faix, K. Rottner, Nature Communications 8 (2017)."},"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"publisher":"Nature Publishing Group","author":[{"full_name":"Kage, Frieda","last_name":"Kage","first_name":"Frieda"},{"first_name":"Moritz","full_name":"Winterhoff, Moritz","last_name":"Winterhoff"},{"last_name":"Dimchev","full_name":"Dimchev, Vanessa","first_name":"Vanessa"},{"last_name":"Müller","full_name":"Müller, Jan","id":"AD07FDB4-0F61-11EA-8158-C4CC64CEAA8D","first_name":"Jan"},{"full_name":"Thalheim, Tobias","last_name":"Thalheim","first_name":"Tobias"},{"first_name":"Anika","full_name":"Freise, Anika","last_name":"Freise"},{"last_name":"Brühmann","full_name":"Brühmann, Stefan","first_name":"Stefan"},{"first_name":"Jana","full_name":"Kollasser, Jana","last_name":"Kollasser"},{"last_name":"Block","full_name":"Block, Jennifer","first_name":"Jennifer"},{"first_name":"Georgi A","last_name":"Dimchev","full_name":"Dimchev, Georgi A"},{"last_name":"Geyer","full_name":"Geyer, Matthias","first_name":"Matthias"},{"first_name":"Hams","full_name":"Schnittler, Hams","last_name":"Schnittler"},{"first_name":"Cord","full_name":"Brakebusch, Cord","last_name":"Brakebusch"},{"last_name":"Stradal","full_name":"Stradal, Theresia","first_name":"Theresia"},{"first_name":"Marie","last_name":"Carlier","full_name":"Carlier, Marie"},{"last_name":"Sixt","full_name":"Sixt, Michael K","orcid":"0000-0002-6620-9179","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K"},{"last_name":"Käs","full_name":"Käs, Josef","first_name":"Josef"},{"full_name":"Faix, Jan","last_name":"Faix","first_name":"Jan"},{"full_name":"Rottner, Klemens","last_name":"Rottner","first_name":"Klemens"}],"_id":"659","article_processing_charge":"No","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}],"pubrep_id":"902","date_published":"2017-03-22T00:00:00Z","day":"22","year":"2017","publist_id":"7075","status":"public","file":[{"access_level":"open_access","date_updated":"2020-07-14T12:47:34Z","date_created":"2018-12-12T10:14:21Z","file_size":9523746,"checksum":"dae30190291c3630e8102d8714a8d23e","content_type":"application/pdf","file_name":"IST-2017-902-v1+1_Kage_et_al-2017-Nature_Communications.pdf","creator":"system","file_id":"5072","relation":"main_file"}],"volume":8,"file_date_updated":"2020-07-14T12:47:34Z"},{"date_published":"2017-04-28T00:00:00Z","day":"28","year":"2017","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}],"_id":"668","article_processing_charge":"No","author":[{"first_name":"Markus","full_name":"Horsthemke, Markus","last_name":"Horsthemke"},{"first_name":"Anne","full_name":"Bachg, Anne","last_name":"Bachg"},{"full_name":"Groll, Katharina","last_name":"Groll","first_name":"Katharina"},{"first_name":"Sven","full_name":"Moyzio, Sven","last_name":"Moyzio"},{"first_name":"Barbara","last_name":"Müther","full_name":"Müther, Barbara"},{"last_name":"Hemkemeyer","full_name":"Hemkemeyer, Sandra","first_name":"Sandra"},{"last_name":"Wedlich Söldner","full_name":"Wedlich Söldner, Roland","first_name":"Roland"},{"full_name":"Sixt, Michael K","last_name":"Sixt","first_name":"Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-6620-9179"},{"full_name":"Tacke, Sebastian","last_name":"Tacke","first_name":"Sebastian"},{"last_name":"Bähler","full_name":"Bähler, Martin","first_name":"Martin"},{"full_name":"Hanley, Peter","last_name":"Hanley","first_name":"Peter"}],"publisher":"American Society for Biochemistry and Molecular Biology","volume":292,"file_date_updated":"2020-07-14T12:47:37Z","status":"public","file":[{"relation":"main_file","file_id":"6971","creator":"dernst","checksum":"d488162874326a4bb056065fa549dc4a","content_type":"application/pdf","file_name":"2017_JBC_Horsthemke.pdf","file_size":5647880,"date_created":"2019-10-24T15:25:42Z","date_updated":"2020-07-14T12:47:37Z","access_level":"open_access"}],"publist_id":"7059","has_accepted_license":"1","publication_identifier":{"issn":["0021-9258"]},"issue":"17","article_type":"original","citation":{"mla":"Horsthemke, Markus, et al. “Multiple Roles of Filopodial Dynamics in Particle Capture and Phagocytosis and Phenotypes of Cdc42 and Myo10 Deletion.” <i>Journal of Biological Chemistry</i>, vol. 292, no. 17, American Society for Biochemistry and Molecular Biology, 2017, pp. 7258–73, doi:<a href=\"https://doi.org/10.1074/jbc.M116.766923\">10.1074/jbc.M116.766923</a>.","ieee":"M. Horsthemke <i>et al.</i>, “Multiple roles of filopodial dynamics in particle capture and phagocytosis and phenotypes of Cdc42 and Myo10 deletion,” <i>Journal of Biological Chemistry</i>, vol. 292, no. 17. American Society for Biochemistry and Molecular Biology, pp. 7258–7273, 2017.","apa":"Horsthemke, M., Bachg, A., Groll, K., Moyzio, S., Müther, B., Hemkemeyer, S., … Hanley, P. (2017). Multiple roles of filopodial dynamics in particle capture and phagocytosis and phenotypes of Cdc42 and Myo10 deletion. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry and Molecular Biology. <a href=\"https://doi.org/10.1074/jbc.M116.766923\">https://doi.org/10.1074/jbc.M116.766923</a>","short":"M. Horsthemke, A. Bachg, K. Groll, S. Moyzio, B. Müther, S. Hemkemeyer, R. Wedlich Söldner, M.K. Sixt, S. Tacke, M. Bähler, P. Hanley, Journal of Biological Chemistry 292 (2017) 7258–7273.","chicago":"Horsthemke, Markus, Anne Bachg, Katharina Groll, Sven Moyzio, Barbara Müther, Sandra Hemkemeyer, Roland Wedlich Söldner, et al. “Multiple Roles of Filopodial Dynamics in Particle Capture and Phagocytosis and Phenotypes of Cdc42 and Myo10 Deletion.” <i>Journal of Biological Chemistry</i>. American Society for Biochemistry and Molecular Biology, 2017. <a href=\"https://doi.org/10.1074/jbc.M116.766923\">https://doi.org/10.1074/jbc.M116.766923</a>.","ista":"Horsthemke M, Bachg A, Groll K, Moyzio S, Müther B, Hemkemeyer S, Wedlich Söldner R, Sixt MK, Tacke S, Bähler M, Hanley P. 2017. Multiple roles of filopodial dynamics in particle capture and phagocytosis and phenotypes of Cdc42 and Myo10 deletion. Journal of Biological Chemistry. 292(17), 7258–7273.","ama":"Horsthemke M, Bachg A, Groll K, et al. Multiple roles of filopodial dynamics in particle capture and phagocytosis and phenotypes of Cdc42 and Myo10 deletion. <i>Journal of Biological Chemistry</i>. 2017;292(17):7258-7273. doi:<a href=\"https://doi.org/10.1074/jbc.M116.766923\">10.1074/jbc.M116.766923</a>"},"quality_controlled":"1","type":"journal_article","language":[{"iso":"eng"}],"oa_version":"Published Version","date_updated":"2025-09-11T07:03:17Z","publication_status":"published","scopus_import":"1","external_id":{"isi":["000400478300035"]},"title":"Multiple roles of filopodial dynamics in particle capture and phagocytosis and phenotypes of Cdc42 and Myo10 deletion","abstract":[{"lang":"eng","text":"Macrophage filopodia, finger-like membrane protrusions, were first implicated in phagocytosis more than 100 years ago, but little is still known about the involvement of these actin-dependent structures in particle clearance. Using spinning disk confocal microscopy to image filopodial dynamics in mouse resident Lifeact-EGFP macrophages, we show that filopodia, or filopodia-like structures, support pathogen clearance by multiple means. Filopodia supported the phagocytic uptake of bacterial (Escherichia coli) particles by (i) capturing along the filopodial shaft and surfing toward the cell body, the most common mode of capture; (ii) capturing via the tip followed by retraction; (iii) combinations of surfing and retraction; or (iv) sweeping actions. In addition, filopodia supported the uptake of zymosan (Saccharomyces cerevisiae) particles by (i) providing fixation, (ii) capturing at the tip and filopodia-guided actin anterograde flow with phagocytic cup formation, and (iii) the rapid growth of new protrusions. To explore the role of filopodia-inducing Cdc42, we generated myeloid-restricted Cdc42 knock-out mice. Cdc42-deficient macrophages exhibited rapid phagocytic cup kinetics, but reduced particle clearance, which could be explained by the marked rounded-up morphology of these cells. Macrophages lacking Myo10, thought to act downstream of Cdc42, had normal morphology, motility, and phagocytic cup formation, but displayed markedly reduced filopodia formation. In conclusion, live-cell imaging revealed multiple mechanisms involving macrophage filopodia in particle capture and engulfment. Cdc42 is not critical for filopodia or phagocytic cup formation, but plays a key role in driving macrophage lamellipodial spreading."}],"doi":"10.1074/jbc.M116.766923","date_created":"2018-12-11T11:47:49Z","publication":"Journal of Biological Chemistry","page":"7258 - 7273","month":"04","isi":1,"ddc":["570"],"intvolume":"       292","oa":1},{"scopus_import":"1","publication_status":"published","date_updated":"2025-09-10T14:27:34Z","oa_version":"Published Version","language":[{"iso":"eng"}],"doi":"10.1016/j.celrep.2017.04.027","title":"Locally triggered release of the chemokine CCL21 promotes dendritic cell transmigration across lymphatic endothelia","abstract":[{"lang":"eng","text":"Trafficking cells frequently transmigrate through epithelial and endothelial monolayers. How monolayers cooperate with the penetrating cells to support their transit is poorly understood. We studied dendritic cell (DC) entry into lymphatic capillaries as a model system for transendothelial migration. We find that the chemokine CCL21, which is the decisive guidance cue for intravasation, mainly localizes in the trans-Golgi network and intracellular vesicles of lymphatic endothelial cells. Upon DC transmigration, these Golgi deposits disperse and CCL21 becomes extracellularly enriched at the sites of endothelial cell-cell junctions. When we reconstitute the transmigration process in vitro, we find that secretion of CCL21-positive vesicles is triggered by a DC contact-induced calcium signal, and selective calcium chelation in lymphatic endothelium attenuates transmigration. Altogether, our data demonstrate a chemokine-mediated feedback between DCs and lymphatic endothelium, which facilitates transendothelial migration."}],"external_id":{"isi":["000402124100002"]},"ddc":["570"],"isi":1,"month":"05","corr_author":"1","publication":"Cell Reports","page":"902 - 909","date_created":"2018-12-11T11:47:50Z","oa":1,"intvolume":"        19","publisher":"Cell Press","article_processing_charge":"Yes","_id":"672","author":[{"id":"368EE576-F248-11E8-B48F-1D18A9856A87","first_name":"Kari","orcid":"0000-0001-7829-3518","full_name":"Vaahtomeri, Kari","last_name":"Vaahtomeri"},{"last_name":"Brown","full_name":"Brown, Markus","first_name":"Markus","id":"3DAB9AFC-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Robert","id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-9843-3522","full_name":"Hauschild, Robert","last_name":"Hauschild"},{"id":"4C7D837E-F248-11E8-B48F-1D18A9856A87","first_name":"Ingrid","full_name":"De Vries, Ingrid","last_name":"De Vries"},{"orcid":"0000-0002-1073-744X","first_name":"Alexander F","id":"3B1B77E4-F248-11E8-B48F-1D18A9856A87","last_name":"Leithner","full_name":"Leithner, Alexander F"},{"orcid":"0000-0001-8599-1226","first_name":"Matthias","id":"3C23B994-F248-11E8-B48F-1D18A9856A87","last_name":"Mehling","full_name":"Mehling, Matthias"},{"orcid":"0000-0001-9735-5315","first_name":"Walter","id":"3F99E422-F248-11E8-B48F-1D18A9856A87","last_name":"Kaufmann","full_name":"Kaufmann, Walter"},{"full_name":"Sixt, Michael K","last_name":"Sixt","first_name":"Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-6620-9179"}],"department":[{"_id":"MiSi"},{"_id":"Bio"},{"_id":"EM-Fac"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","day":"02","year":"2017","pubrep_id":"900","date_published":"2017-05-02T00:00:00Z","publist_id":"7052","license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","file":[{"date_updated":"2020-07-14T12:47:38Z","access_level":"open_access","date_created":"2018-12-12T10:14:54Z","file_size":2248814,"creator":"system","file_name":"IST-2017-900-v1+1_1-s2.0-S2211124717305211-main.pdf","content_type":"application/pdf","checksum":"8fdddaab1f1d76a6ec9ca94dcb6b07a2","relation":"main_file","file_id":"5109"}],"ec_funded":1,"status":"public","volume":19,"file_date_updated":"2020-07-14T12:47:38Z","issue":"5","publication_identifier":{"issn":["2211-1247"]},"has_accepted_license":"1","type":"journal_article","project":[{"grant_number":"281556","call_identifier":"FP7","_id":"25A603A2-B435-11E9-9278-68D0E5697425","name":"Cytoskeletal force generation and force transduction of migrating leukocytes"},{"grant_number":"Y 564-B12","call_identifier":"FWF","_id":"25A8E5EA-B435-11E9-9278-68D0E5697425","name":"Cytoskeletal force generation and force transduction of migrating leukocytes"}],"quality_controlled":"1","citation":{"mla":"Vaahtomeri, Kari, et al. “Locally Triggered Release of the Chemokine CCL21 Promotes Dendritic Cell Transmigration across Lymphatic Endothelia.” <i>Cell Reports</i>, vol. 19, no. 5, Cell Press, 2017, pp. 902–09, doi:<a href=\"https://doi.org/10.1016/j.celrep.2017.04.027\">10.1016/j.celrep.2017.04.027</a>.","ista":"Vaahtomeri K, Brown M, Hauschild R, de Vries I, Leithner AF, Mehling M, Kaufmann W, Sixt MK. 2017. Locally triggered release of the chemokine CCL21 promotes dendritic cell transmigration across lymphatic endothelia. Cell Reports. 19(5), 902–909.","ama":"Vaahtomeri K, Brown M, Hauschild R, et al. Locally triggered release of the chemokine CCL21 promotes dendritic cell transmigration across lymphatic endothelia. <i>Cell Reports</i>. 2017;19(5):902-909. doi:<a href=\"https://doi.org/10.1016/j.celrep.2017.04.027\">10.1016/j.celrep.2017.04.027</a>","ieee":"K. Vaahtomeri <i>et al.</i>, “Locally triggered release of the chemokine CCL21 promotes dendritic cell transmigration across lymphatic endothelia,” <i>Cell Reports</i>, vol. 19, no. 5. Cell Press, pp. 902–909, 2017.","apa":"Vaahtomeri, K., Brown, M., Hauschild, R., de Vries, I., Leithner, A. F., Mehling, M., … Sixt, M. K. (2017). Locally triggered release of the chemokine CCL21 promotes dendritic cell transmigration across lymphatic endothelia. <i>Cell Reports</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.celrep.2017.04.027\">https://doi.org/10.1016/j.celrep.2017.04.027</a>","chicago":"Vaahtomeri, Kari, Markus Brown, Robert Hauschild, Ingrid de Vries, Alexander F Leithner, Matthias Mehling, Walter Kaufmann, and Michael K Sixt. “Locally Triggered Release of the Chemokine CCL21 Promotes Dendritic Cell Transmigration across Lymphatic Endothelia.” <i>Cell Reports</i>. Cell Press, 2017. <a href=\"https://doi.org/10.1016/j.celrep.2017.04.027\">https://doi.org/10.1016/j.celrep.2017.04.027</a>.","short":"K. Vaahtomeri, M. Brown, R. Hauschild, I. de Vries, A.F. Leithner, M. Mehling, W. Kaufmann, M.K. Sixt, Cell Reports 19 (2017) 902–909."},"tmp":{"short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode"}},{"_id":"674","author":[{"last_name":"Schwarz","full_name":"Schwarz, Jan","first_name":"Jan","id":"346C1EC6-F248-11E8-B48F-1D18A9856A87"},{"id":"3FD04378-F248-11E8-B48F-1D18A9856A87","first_name":"Veronika","last_name":"Bierbaum","full_name":"Bierbaum, Veronika"},{"orcid":"0000-0001-7829-3518","id":"368EE576-F248-11E8-B48F-1D18A9856A87","first_name":"Kari","last_name":"Vaahtomeri","full_name":"Vaahtomeri, Kari"},{"full_name":"Hauschild, Robert","last_name":"Hauschild","first_name":"Robert","id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-9843-3522"},{"id":"3DAB9AFC-F248-11E8-B48F-1D18A9856A87","first_name":"Markus","last_name":"Brown","full_name":"Brown, Markus"},{"last_name":"De Vries","full_name":"De Vries, Ingrid","first_name":"Ingrid","id":"4C7D837E-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Leithner, Alexander F","last_name":"Leithner","first_name":"Alexander F","id":"3B1B77E4-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-1073-744X"},{"full_name":"Reversat, Anne","last_name":"Reversat","id":"35B76592-F248-11E8-B48F-1D18A9856A87","first_name":"Anne","orcid":"0000-0003-0666-8928"},{"orcid":"0000-0001-5145-4609","id":"4515C308-F248-11E8-B48F-1D18A9856A87","first_name":"Jack","last_name":"Merrin","full_name":"Merrin, Jack"},{"last_name":"Tarrant","full_name":"Tarrant, Teresa","first_name":"Teresa"},{"orcid":"0000-0003-4398-476X","first_name":"Tobias","id":"3E6DB97A-F248-11E8-B48F-1D18A9856A87","last_name":"Bollenbach","full_name":"Bollenbach, Tobias"},{"full_name":"Sixt, Michael K","last_name":"Sixt","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K","orcid":"0000-0002-6620-9179"}],"article_processing_charge":"No","publisher":"Cell Press","day":"09","year":"2017","date_published":"2017-05-09T00:00:00Z","department":[{"_id":"MiSi"},{"_id":"Bio"},{"_id":"NanoFab"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publist_id":"7050","volume":27,"ec_funded":1,"status":"public","issue":"9","publication_identifier":{"issn":["09609822"]},"type":"journal_article","quality_controlled":"1","project":[{"grant_number":"291734","_id":"25681D80-B435-11E9-9278-68D0E5697425","name":"International IST Postdoc Fellowship Programme","call_identifier":"FP7"},{"grant_number":"Y 564-B12","_id":"25A8E5EA-B435-11E9-9278-68D0E5697425","name":"Cytoskeletal force generation and force transduction of migrating leukocytes","call_identifier":"FWF"}],"citation":{"mla":"Schwarz, Jan, et al. “Dendritic Cells Interpret Haptotactic Chemokine Gradients in a Manner Governed by Signal to Noise Ratio and Dependent on GRK6.” <i>Current Biology</i>, vol. 27, no. 9, Cell Press, 2017, pp. 1314–25, doi:<a href=\"https://doi.org/10.1016/j.cub.2017.04.004\">10.1016/j.cub.2017.04.004</a>.","ieee":"J. Schwarz <i>et al.</i>, “Dendritic cells interpret haptotactic chemokine gradients in a manner governed by signal to noise ratio and dependent on GRK6,” <i>Current Biology</i>, vol. 27, no. 9. Cell Press, pp. 1314–1325, 2017.","apa":"Schwarz, J., Bierbaum, V., Vaahtomeri, K., Hauschild, R., Brown, M., de Vries, I., … Sixt, M. K. (2017). Dendritic cells interpret haptotactic chemokine gradients in a manner governed by signal to noise ratio and dependent on GRK6. <i>Current Biology</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.cub.2017.04.004\">https://doi.org/10.1016/j.cub.2017.04.004</a>","chicago":"Schwarz, Jan, Veronika Bierbaum, Kari Vaahtomeri, Robert Hauschild, Markus Brown, Ingrid de Vries, Alexander F Leithner, et al. “Dendritic Cells Interpret Haptotactic Chemokine Gradients in a Manner Governed by Signal to Noise Ratio and Dependent on GRK6.” <i>Current Biology</i>. Cell Press, 2017. <a href=\"https://doi.org/10.1016/j.cub.2017.04.004\">https://doi.org/10.1016/j.cub.2017.04.004</a>.","short":"J. Schwarz, V. Bierbaum, K. Vaahtomeri, R. Hauschild, M. Brown, I. de Vries, A.F. Leithner, A. Reversat, J. Merrin, T. Tarrant, M.T. Bollenbach, M.K. Sixt, Current Biology 27 (2017) 1314–1325.","ista":"Schwarz J, Bierbaum V, Vaahtomeri K, Hauschild R, Brown M, de Vries I, Leithner AF, Reversat A, Merrin J, Tarrant T, Bollenbach MT, Sixt MK. 2017. Dendritic cells interpret haptotactic chemokine gradients in a manner governed by signal to noise ratio and dependent on GRK6. Current Biology. 27(9), 1314–1325.","ama":"Schwarz J, Bierbaum V, Vaahtomeri K, et al. Dendritic cells interpret haptotactic chemokine gradients in a manner governed by signal to noise ratio and dependent on GRK6. <i>Current Biology</i>. 2017;27(9):1314-1325. doi:<a href=\"https://doi.org/10.1016/j.cub.2017.04.004\">10.1016/j.cub.2017.04.004</a>"},"date_updated":"2025-09-10T14:26:47Z","publication_status":"published","scopus_import":"1","oa_version":"None","language":[{"iso":"eng"}],"doi":"10.1016/j.cub.2017.04.004","external_id":{"isi":["000400741700021"]},"title":"Dendritic cells interpret haptotactic chemokine gradients in a manner governed by signal to noise ratio and dependent on GRK6","abstract":[{"lang":"eng","text":"Navigation of cells along gradients of guidance cues is a determining step in many developmental and immunological processes. Gradients can either be soluble or immobilized to tissues as demonstrated for the haptotactic migration of dendritic cells (DCs) toward higher concentrations of immobilized chemokine CCL21. To elucidate how gradient characteristics govern cellular response patterns, we here introduce an in vitro system allowing to track migratory responses of DCs to precisely controlled immobilized gradients of CCL21. We find that haptotactic sensing depends on the absolute CCL21 concentration and local steepness of the gradient, consistent with a scenario where DC directionality is governed by the signal-to-noise ratio of CCL21 binding to the receptor CCR7. We find that the conditions for optimal DC guidance are perfectly provided by the CCL21 gradients we measure in vivo. Furthermore, we find that CCR7 signal termination by the G-protein-coupled receptor kinase 6 (GRK6) is crucial for haptotactic but dispensable for chemotactic CCL21 gradient sensing in vitro and confirm those observations in vivo. These findings suggest that stable, tissue-bound CCL21 gradients as sustainable “roads” ensure optimal guidance in vivo."}],"corr_author":"1","isi":1,"month":"05","page":"1314 - 1325","publication":"Current Biology","date_created":"2018-12-11T11:47:51Z","intvolume":"        27"},{"publication_identifier":{"issn":["2211-1247"]},"has_accepted_license":"1","issue":"7","tmp":{"short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode"},"citation":{"short":"C. Lademann, J. Renkawitz, B. Pfander, S. Jentsch, Cell Reports 19 (2017) 1294–1303.","chicago":"Lademann, Claudio, Jörg Renkawitz, Boris Pfander, and Stefan Jentsch. “The INO80 Complex Removes H2A.Z to Promote Presynaptic Filament Formation during Homologous Recombination.” <i>Cell Reports</i>. Cell Press, 2017. <a href=\"https://doi.org/10.1016/j.celrep.2017.04.051\">https://doi.org/10.1016/j.celrep.2017.04.051</a>.","apa":"Lademann, C., Renkawitz, J., Pfander, B., &#38; Jentsch, S. (2017). The INO80 complex removes H2A.Z to promote presynaptic filament formation during homologous recombination. <i>Cell Reports</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.celrep.2017.04.051\">https://doi.org/10.1016/j.celrep.2017.04.051</a>","ieee":"C. Lademann, J. Renkawitz, B. Pfander, and S. Jentsch, “The INO80 complex removes H2A.Z to promote presynaptic filament formation during homologous recombination,” <i>Cell Reports</i>, vol. 19, no. 7. Cell Press, pp. 1294–1303, 2017.","ama":"Lademann C, Renkawitz J, Pfander B, Jentsch S. The INO80 complex removes H2A.Z to promote presynaptic filament formation during homologous recombination. <i>Cell Reports</i>. 2017;19(7):1294-1303. doi:<a href=\"https://doi.org/10.1016/j.celrep.2017.04.051\">10.1016/j.celrep.2017.04.051</a>","ista":"Lademann C, Renkawitz J, Pfander B, Jentsch S. 2017. The INO80 complex removes H2A.Z to promote presynaptic filament formation during homologous recombination. Cell Reports. 19(7), 1294–1303.","mla":"Lademann, Claudio, et al. “The INO80 Complex Removes H2A.Z to Promote Presynaptic Filament Formation during Homologous Recombination.” <i>Cell Reports</i>, vol. 19, no. 7, Cell Press, 2017, pp. 1294–303, doi:<a href=\"https://doi.org/10.1016/j.celrep.2017.04.051\">10.1016/j.celrep.2017.04.051</a>."},"type":"journal_article","quality_controlled":"1","year":"2017","day":"16","date_published":"2017-05-16T00:00:00Z","pubrep_id":"899","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}],"_id":"677","article_processing_charge":"No","author":[{"last_name":"Lademann","full_name":"Lademann, Claudio","first_name":"Claudio"},{"id":"3F0587C8-F248-11E8-B48F-1D18A9856A87","first_name":"Jörg","orcid":"0000-0003-2856-3369","full_name":"Renkawitz, Jörg","last_name":"Renkawitz"},{"first_name":"Boris","last_name":"Pfander","full_name":"Pfander, Boris"},{"full_name":"Jentsch, Stefan","last_name":"Jentsch","first_name":"Stefan"}],"publisher":"Cell Press","file_date_updated":"2020-07-14T12:47:40Z","volume":19,"file":[{"file_size":3005610,"date_created":"2018-12-12T10:15:48Z","access_level":"open_access","date_updated":"2020-07-14T12:47:40Z","file_id":"5171","relation":"main_file","checksum":"efc7287d9c6354983cb151880e9ad72a","file_name":"IST-2017-899-v1+1_1-s2.0-S2211124717305454-main.pdf","content_type":"application/pdf","creator":"system"}],"status":"public","publist_id":"7046","page":"1294 - 1303","publication":"Cell Reports","date_created":"2018-12-11T11:47:52Z","ddc":["570"],"isi":1,"month":"05","intvolume":"        19","oa":1,"oa_version":"Published Version","language":[{"iso":"eng"}],"date_updated":"2025-09-10T14:23:55Z","publication_status":"published","scopus_import":"1","external_id":{"isi":["000402125100002"]},"title":"The INO80 complex removes H2A.Z to promote presynaptic filament formation during homologous recombination","abstract":[{"text":"The INO80 complex (INO80-C) is an evolutionarily conserved nucleosome remodeler that acts in transcription, replication, and genome stability. It is required for resistance against genotoxic agents and is involved in the repair of DNA double-strand breaks (DSBs) by homologous recombination (HR). However, the causes of the HR defect in INO80-C mutant cells are controversial. Here, we unite previous findings using a system to study HR with high spatial resolution in budding yeast. We find that INO80-C has at least two distinct functions during HR—DNA end resection and presynaptic filament formation. Importantly, the second function is linked to the histone variant H2A.Z. In the absence of H2A.Z, presynaptic filament formation and HR are restored in INO80-C-deficient mutants, suggesting that presynaptic filament formation is the crucial INO80-C function during HR.","lang":"eng"}],"doi":"10.1016/j.celrep.2017.04.051"},{"date_created":"2018-12-11T11:47:58Z","publication":"Journal of Cell Science","page":"2172 - 2184","month":"07","ddc":["570"],"isi":1,"intvolume":"       130","oa":1,"language":[{"iso":"eng"}],"oa_version":"Published Version","scopus_import":"1","publication_status":"published","date_updated":"2025-09-10T11:13:35Z","title":"A dual phenotype of MDA MB 468 cancer cells reveals mutual regulation of tensin3 and adhesion plasticity","abstract":[{"text":"A change regarding the extent of adhesion - hereafter referred to as adhesion plasticity - between adhesive and less-adhesive states of mammalian cells is important for their behavior. To investigate adhesion plasticity, we have selected a stable isogenic subpopulation of human MDA-MB-468 breast carcinoma cells growing in suspension. These suspension cells are unable to re-adhere to various matrices or to contract three-dimensional collagen lattices. By using transcriptome analysis, we identified the focal adhesion protein tensin3 (Tns3) as a determinant of adhesion plasticity. Tns3 is strongly reduced at mRNA and protein levels in suspension cells. Furthermore, by transiently challenging breast cancer cells to grow under non-adherent conditions markedly reduces Tns3 protein expression, which is regained upon re-adhesion. Stable knockdown of Tns3 in parental MDA-MB-468 cells results in defective adhesion, spreading and migration. Tns3-knockdown cells display impaired structure and dynamics of focal adhesion complexes as determined by immunostaining. Restoration of Tns3 protein expression in suspension cells partially rescues adhesion and focal contact composition. Our work identifies Tns3 as a crucial focal adhesion component regulated by, and functionally contributing to, the switch between adhesive and non-adhesive states in MDA-MB-468 cancer cells.","lang":"eng"}],"external_id":{"pmid":["28515231"],"isi":["000405612200009"]},"doi":"10.1242/jcs.200899","has_accepted_license":"1","publication_identifier":{"issn":["0021-9533"]},"issue":"13","citation":{"mla":"Veß, Astrid, et al. “A Dual Phenotype of MDA MB 468 Cancer Cells Reveals Mutual Regulation of Tensin3 and Adhesion Plasticity.” <i>Journal of Cell Science</i>, vol. 130, no. 13, Company of Biologists, 2017, pp. 2172–84, doi:<a href=\"https://doi.org/10.1242/jcs.200899\">10.1242/jcs.200899</a>.","chicago":"Veß, Astrid, Ulrich Blache, Laura Leitner, Angela Kurz, Anja Ehrenpfordt, Michael K Sixt, and Guido Posern. “A Dual Phenotype of MDA MB 468 Cancer Cells Reveals Mutual Regulation of Tensin3 and Adhesion Plasticity.” <i>Journal of Cell Science</i>. Company of Biologists, 2017. <a href=\"https://doi.org/10.1242/jcs.200899\">https://doi.org/10.1242/jcs.200899</a>.","short":"A. Veß, U. Blache, L. Leitner, A. Kurz, A. Ehrenpfordt, M.K. Sixt, G. Posern, Journal of Cell Science 130 (2017) 2172–2184.","apa":"Veß, A., Blache, U., Leitner, L., Kurz, A., Ehrenpfordt, A., Sixt, M. K., &#38; Posern, G. (2017). A dual phenotype of MDA MB 468 cancer cells reveals mutual regulation of tensin3 and adhesion plasticity. <i>Journal of Cell Science</i>. Company of Biologists. <a href=\"https://doi.org/10.1242/jcs.200899\">https://doi.org/10.1242/jcs.200899</a>","ieee":"A. Veß <i>et al.</i>, “A dual phenotype of MDA MB 468 cancer cells reveals mutual regulation of tensin3 and adhesion plasticity,” <i>Journal of Cell Science</i>, vol. 130, no. 13. Company of Biologists, pp. 2172–2184, 2017.","ama":"Veß A, Blache U, Leitner L, et al. A dual phenotype of MDA MB 468 cancer cells reveals mutual regulation of tensin3 and adhesion plasticity. <i>Journal of Cell Science</i>. 2017;130(13):2172-2184. doi:<a href=\"https://doi.org/10.1242/jcs.200899\">10.1242/jcs.200899</a>","ista":"Veß A, Blache U, Leitner L, Kurz A, Ehrenpfordt A, Sixt MK, Posern G. 2017. A dual phenotype of MDA MB 468 cancer cells reveals mutual regulation of tensin3 and adhesion plasticity. Journal of Cell Science. 130(13), 2172–2184."},"article_type":"original","quality_controlled":"1","type":"journal_article","pmid":1,"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}],"date_published":"2017-07-01T00:00:00Z","day":"01","year":"2017","publisher":"Company of Biologists","_id":"694","article_processing_charge":"No","author":[{"first_name":"Astrid","last_name":"Veß","full_name":"Veß, Astrid"},{"last_name":"Blache","full_name":"Blache, Ulrich","first_name":"Ulrich"},{"first_name":"Laura","last_name":"Leitner","full_name":"Leitner, Laura"},{"full_name":"Kurz, Angela","last_name":"Kurz","first_name":"Angela"},{"first_name":"Anja","full_name":"Ehrenpfordt, Anja","last_name":"Ehrenpfordt"},{"last_name":"Sixt","full_name":"Sixt, Michael K","orcid":"0000-0002-6620-9179","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K"},{"full_name":"Posern, Guido","last_name":"Posern","first_name":"Guido"}],"status":"public","file":[{"file_name":"2017_CellScience_Vess.pdf","content_type":"application/pdf","checksum":"42c81a0a4fc3128883b391c3af3f74bc","creator":"dernst","file_id":"6966","relation":"main_file","access_level":"open_access","date_updated":"2020-07-14T12:47:45Z","file_size":10847596,"date_created":"2019-10-24T09:43:56Z"}],"file_date_updated":"2020-07-14T12:47:45Z","volume":130,"publist_id":"7008"},{"publication_identifier":{"issn":["0092-8674"]},"issue":"1","citation":{"mla":"Mueller, Jan, et al. “Load Adaptation of Lamellipodial Actin Networks.” <i>Cell</i>, vol. 171, no. 1, Cell Press, 2017, pp. 188–200, doi:<a href=\"https://doi.org/10.1016/j.cell.2017.07.051\">10.1016/j.cell.2017.07.051</a>.","chicago":"Mueller, Jan, Gregory Szep, Maria Nemethova, Ingrid de Vries, Arnon Lieber, Christoph Winkler, Karsten Kruse, et al. “Load Adaptation of Lamellipodial Actin Networks.” <i>Cell</i>. Cell Press, 2017. <a href=\"https://doi.org/10.1016/j.cell.2017.07.051\">https://doi.org/10.1016/j.cell.2017.07.051</a>.","short":"J. Mueller, G. Szep, M. Nemethova, I. de Vries, A. Lieber, C. Winkler, K. Kruse, J. Small, C. Schmeiser, K. Keren, R. Hauschild, M.K. Sixt, Cell 171 (2017) 188–200.","ieee":"J. Mueller <i>et al.</i>, “Load adaptation of lamellipodial actin networks,” <i>Cell</i>, vol. 171, no. 1. Cell Press, pp. 188–200, 2017.","apa":"Mueller, J., Szep, G., Nemethova, M., de Vries, I., Lieber, A., Winkler, C., … Sixt, M. K. (2017). Load adaptation of lamellipodial actin networks. <i>Cell</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.cell.2017.07.051\">https://doi.org/10.1016/j.cell.2017.07.051</a>","ama":"Mueller J, Szep G, Nemethova M, et al. Load adaptation of lamellipodial actin networks. <i>Cell</i>. 2017;171(1):188-200. doi:<a href=\"https://doi.org/10.1016/j.cell.2017.07.051\">10.1016/j.cell.2017.07.051</a>","ista":"Mueller J, Szep G, Nemethova M, de Vries I, Lieber A, Winkler C, Kruse K, Small J, Schmeiser C, Keren K, Hauschild R, Sixt MK. 2017. Load adaptation of lamellipodial actin networks. Cell. 171(1), 188–200."},"type":"journal_article","quality_controlled":"1","project":[{"name":"Modeling of Polarization and Motility of Leukocytes in Three-Dimensional Environments","_id":"25AD6156-B435-11E9-9278-68D0E5697425","grant_number":"LS13-029"},{"call_identifier":"FP7","_id":"25A603A2-B435-11E9-9278-68D0E5697425","name":"Cytoskeletal force generation and force transduction of migrating leukocytes","grant_number":"281556"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","department":[{"_id":"MiSi"},{"_id":"Bio"}],"year":"2017","day":"21","date_published":"2017-09-21T00:00:00Z","publisher":"Cell Press","_id":"727","article_processing_charge":"No","author":[{"first_name":"Jan","full_name":"Mueller, Jan","last_name":"Mueller"},{"first_name":"Gregory","id":"4BFB7762-F248-11E8-B48F-1D18A9856A87","full_name":"Szep, Gregory","last_name":"Szep"},{"full_name":"Nemethova, Maria","last_name":"Nemethova","first_name":"Maria","id":"34E27F1C-F248-11E8-B48F-1D18A9856A87"},{"last_name":"De Vries","full_name":"De Vries, Ingrid","id":"4C7D837E-F248-11E8-B48F-1D18A9856A87","first_name":"Ingrid"},{"full_name":"Lieber, Arnon","last_name":"Lieber","first_name":"Arnon"},{"full_name":"Winkler, Christoph","last_name":"Winkler","first_name":"Christoph"},{"last_name":"Kruse","full_name":"Kruse, Karsten","first_name":"Karsten"},{"first_name":"John","last_name":"Small","full_name":"Small, John"},{"last_name":"Schmeiser","full_name":"Schmeiser, Christian","first_name":"Christian"},{"full_name":"Keren, Kinneret","last_name":"Keren","first_name":"Kinneret"},{"last_name":"Hauschild","full_name":"Hauschild, Robert","orcid":"0000-0001-9843-3522","first_name":"Robert","id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Sixt, Michael K","last_name":"Sixt","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K","orcid":"0000-0002-6620-9179"}],"ec_funded":1,"status":"public","volume":171,"publist_id":"6951","page":"188 - 200","publication":"Cell","date_created":"2018-12-11T11:48:10Z","isi":1,"month":"09","corr_author":"1","intvolume":"       171","oa_version":"None","language":[{"iso":"eng"}],"scopus_import":"1","publication_status":"published","date_updated":"2025-07-10T11:54:27Z","title":"Load adaptation of lamellipodial actin networks","abstract":[{"lang":"eng","text":"Actin filaments polymerizing against membranes power endocytosis, vesicular traffic, and cell motility. In vitro reconstitution studies suggest that the structure and the dynamics of actin networks respond to mechanical forces. We demonstrate that lamellipodial actin of migrating cells responds to mechanical load when membrane tension is modulated. In a steady state, migrating cell filaments assume the canonical dendritic geometry, defined by Arp2/3-generated 70° branch points. Increased tension triggers a dense network with a broadened range of angles, whereas decreased tension causes a shift to a sparse configuration dominated by filaments growing perpendicularly to the plasma membrane. We show that these responses emerge from the geometry of branched actin: when load per filament decreases, elongation speed increases and perpendicular filaments gradually outcompete others because they polymerize the shortest distance to the membrane, where they are protected from capping. This network-intrinsic geometrical adaptation mechanism tunes protrusive force in response to mechanical load."}],"acknowledged_ssus":[{"_id":"ScienComp"}],"external_id":{"isi":["000411331800020"]},"doi":"10.1016/j.cell.2017.07.051"},{"citation":{"ista":"Assen FP, Sixt MK. 2017. The dynamic cytokine niche. Immunity. 46(4), 519–520.","ama":"Assen FP, Sixt MK. The dynamic cytokine niche. <i>Immunity</i>. 2017;46(4):519-520. doi:<a href=\"https://doi.org/10.1016/j.immuni.2017.04.006\">10.1016/j.immuni.2017.04.006</a>","ieee":"F. P. Assen and M. K. Sixt, “The dynamic cytokine niche,” <i>Immunity</i>, vol. 46, no. 4. Cell Press, pp. 519–520, 2017.","apa":"Assen, F. P., &#38; Sixt, M. K. (2017). The dynamic cytokine niche. <i>Immunity</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.immuni.2017.04.006\">https://doi.org/10.1016/j.immuni.2017.04.006</a>","chicago":"Assen, Frank P, and Michael K Sixt. “The Dynamic Cytokine Niche.” <i>Immunity</i>. Cell Press, 2017. <a href=\"https://doi.org/10.1016/j.immuni.2017.04.006\">https://doi.org/10.1016/j.immuni.2017.04.006</a>.","short":"F.P. Assen, M.K. Sixt, Immunity 46 (2017) 519–520.","mla":"Assen, Frank P., and Michael K. Sixt. “The Dynamic Cytokine Niche.” <i>Immunity</i>, vol. 46, no. 4, Cell Press, 2017, pp. 519–20, doi:<a href=\"https://doi.org/10.1016/j.immuni.2017.04.006\">10.1016/j.immuni.2017.04.006</a>."},"type":"journal_article","quality_controlled":"1","publication_identifier":{"issn":["1074-7613"]},"issue":"4","related_material":{"record":[{"id":"6947","status":"public","relation":"dissertation_contains"}]},"status":"public","volume":46,"publist_id":"7065","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}],"day":"18","year":"2017","date_published":"2017-04-18T00:00:00Z","publisher":"Cell Press","_id":"664","article_processing_charge":"No","author":[{"full_name":"Assen, Frank P","last_name":"Assen","first_name":"Frank P","id":"3A8E7F24-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-3470-6119"},{"last_name":"Sixt","full_name":"Sixt, Michael K","orcid":"0000-0002-6620-9179","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K"}],"intvolume":"        46","publication":"Immunity","page":"519 - 520","date_created":"2018-12-11T11:47:47Z","isi":1,"month":"04","corr_author":"1","abstract":[{"lang":"eng","text":"Immune cells communicate using cytokine signals, but the quantitative rules of this communication aren't clear. In this issue of Immunity, Oyler-Yaniv et al. (2017) suggest that the distribution of a cytokine within a lymphatic organ is primarily governed by the local density of cells consuming it."}],"title":"The dynamic cytokine niche","external_id":{"isi":["000399451100002"]},"doi":"10.1016/j.immuni.2017.04.006","oa_version":"None","language":[{"iso":"eng"}],"scopus_import":"1","date_updated":"2026-06-05T22:34:18Z","publication_status":"published"},{"publication_identifier":{"issn":["0021-9738"]},"issue":"6","main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5451238/","open_access":"1"}],"related_material":{"record":[{"status":"public","relation":"dissertation_contains","id":"12401"}]},"citation":{"mla":"Ebner, Florian, et al. “The RNA-Binding Protein Tristetraprolin Schedules Apoptosis of Pathogen-Engaged Neutrophils during Bacterial Infection.” <i>The Journal of Clinical Investigation</i>, vol. 127, no. 6, American Society for Clinical Investigation, 2017, pp. 2051–65, doi:<a href=\"https://doi.org/10.1172/JCI80631\">10.1172/JCI80631</a>.","ama":"Ebner F, Sedlyarov V, Tasciyan S, et al. The RNA-binding protein tristetraprolin schedules apoptosis of pathogen-engaged neutrophils during bacterial infection. <i>The Journal of Clinical Investigation</i>. 2017;127(6):2051-2065. doi:<a href=\"https://doi.org/10.1172/JCI80631\">10.1172/JCI80631</a>","ista":"Ebner F, Sedlyarov V, Tasciyan S, Ivin M, Kratochvill F, Gratz N, Kenner L, Villunger A, Sixt MK, Kovarik P. 2017. The RNA-binding protein tristetraprolin schedules apoptosis of pathogen-engaged neutrophils during bacterial infection. The Journal of Clinical Investigation. 127(6), 2051–2065.","apa":"Ebner, F., Sedlyarov, V., Tasciyan, S., Ivin, M., Kratochvill, F., Gratz, N., … Kovarik, P. (2017). The RNA-binding protein tristetraprolin schedules apoptosis of pathogen-engaged neutrophils during bacterial infection. <i>The Journal of Clinical Investigation</i>. American Society for Clinical Investigation. <a href=\"https://doi.org/10.1172/JCI80631\">https://doi.org/10.1172/JCI80631</a>","ieee":"F. Ebner <i>et al.</i>, “The RNA-binding protein tristetraprolin schedules apoptosis of pathogen-engaged neutrophils during bacterial infection,” <i>The Journal of Clinical Investigation</i>, vol. 127, no. 6. American Society for Clinical Investigation, pp. 2051–2065, 2017.","chicago":"Ebner, Florian, Vitaly Sedlyarov, Saren Tasciyan, Masa Ivin, Franz Kratochvill, Nina Gratz, Lukas Kenner, Andreas Villunger, Michael K Sixt, and Pavel Kovarik. “The RNA-Binding Protein Tristetraprolin Schedules Apoptosis of Pathogen-Engaged Neutrophils during Bacterial Infection.” <i>The Journal of Clinical Investigation</i>. American Society for Clinical Investigation, 2017. <a href=\"https://doi.org/10.1172/JCI80631\">https://doi.org/10.1172/JCI80631</a>.","short":"F. Ebner, V. Sedlyarov, S. Tasciyan, M. Ivin, F. Kratochvill, N. Gratz, L. Kenner, A. Villunger, M.K. Sixt, P. Kovarik, The Journal of Clinical Investigation 127 (2017) 2051–2065."},"project":[{"grant_number":"T00817-B21","name":"The biochemical basis of PAR polarization","_id":"25985A36-B435-11E9-9278-68D0E5697425","call_identifier":"FWF"},{"grant_number":"P27201-B22","_id":"25E9AF9E-B435-11E9-9278-68D0E5697425","name":"Revealing the mechanisms underlying drug interactions","call_identifier":"FWF"}],"quality_controlled":"1","type":"journal_article","pmid":1,"department":[{"_id":"MiSi"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","date_published":"2017-06-01T00:00:00Z","day":"01","year":"2017","publisher":"American Society for Clinical Investigation","_id":"679","article_processing_charge":"No","author":[{"first_name":"Florian","full_name":"Ebner, Florian","last_name":"Ebner"},{"last_name":"Sedlyarov","full_name":"Sedlyarov, Vitaly","first_name":"Vitaly"},{"orcid":"0000-0003-1671-393X","id":"4323B49C-F248-11E8-B48F-1D18A9856A87","first_name":"Saren","last_name":"Tasciyan","full_name":"Tasciyan, Saren"},{"last_name":"Ivin","full_name":"Ivin, Masa","first_name":"Masa"},{"first_name":"Franz","full_name":"Kratochvill, Franz","last_name":"Kratochvill"},{"first_name":"Nina","last_name":"Gratz","full_name":"Gratz, Nina"},{"first_name":"Lukas","last_name":"Kenner","full_name":"Kenner, Lukas"},{"full_name":"Villunger, Andreas","last_name":"Villunger","first_name":"Andreas"},{"last_name":"Sixt","full_name":"Sixt, Michael K","orcid":"0000-0002-6620-9179","first_name":"Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Pavel","full_name":"Kovarik, Pavel","last_name":"Kovarik"}],"status":"public","volume":127,"acknowledgement":"This work was supported by grants from the Austrian Science Fund (FWF) (P27538-B21, I1621-B22, and SFB 43, to PK); by funding from the European Union Seventh Framework Programme Marie Curie Initial Training Networks (FP7-PEOPLE-2012-ITN) for the project INBIONET (INfection BIOlogy Training NETwork under grant agreement PITN-GA-2012-316682; and by a joint research cluster initiative of the University of Vienna and the Medical University of Vienna.","publist_id":"7038","date_created":"2018-12-11T11:47:53Z","publication":"The Journal of Clinical Investigation","page":"2051 - 2065","month":"06","isi":1,"intvolume":"       127","oa":1,"language":[{"iso":"eng"}],"oa_version":"Submitted Version","scopus_import":"1","date_updated":"2026-06-05T22:34:43Z","publication_status":"published","abstract":[{"text":"Protective responses against pathogens require a rapid mobilization of resting neutrophils and the timely removal of activated ones. Neutrophils are exceptionally short-lived leukocytes, yet it remains unclear whether the lifespan of pathogen-engaged neutrophils is regulated differently from that in the circulating steady-state pool. Here, we have found that under homeostatic conditions, the mRNA-destabilizing protein tristetraprolin (TTP) regulates apoptosis and the numbers of activated infiltrating murine neutrophils but not neutrophil cellularity. Activated TTP-deficient neutrophils exhibited decreased apoptosis and enhanced accumulation at the infection site. In the context of myeloid-specific deletion of Ttp, the potentiation of neutrophil deployment protected mice against lethal soft tissue infection with Streptococcus pyogenes and prevented bacterial dissemination. Neutrophil transcriptome analysis revealed that decreased apoptosis of TTP-deficient neutrophils was specifically associated with elevated expression of myeloid cell leukemia 1 (Mcl1) but not other antiapoptotic B cell leukemia/ lymphoma 2 (Bcl2) family members. Higher Mcl1 expression resulted from stabilization of Mcl1 mRNA in the absence of TTP. The low apoptosis rate of infiltrating TTP-deficient neutrophils was comparable to that of transgenic Mcl1-overexpressing neutrophils. Our study demonstrates that posttranscriptional gene regulation by TTP schedules the termination of the antimicrobial engagement of neutrophils. The balancing role of TTP comes at the cost of an increased risk of bacterial infections.","lang":"eng"}],"title":"The RNA-binding protein tristetraprolin schedules apoptosis of pathogen-engaged neutrophils during bacterial infection","external_id":{"pmid":["28504646"],"isi":["000402620800008"]},"doi":"10.1172/JCI80631"},{"_id":"1150","article_processing_charge":"No","author":[{"first_name":"Jörg","id":"3F0587C8-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-2856-3369","full_name":"Renkawitz, Jörg","last_name":"Renkawitz"},{"orcid":"0000-0002-6620-9179","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K","last_name":"Sixt","full_name":"Sixt, Michael K"}],"publisher":"Cell Press","year":"2016","day":"12","date_published":"2016-09-12T00:00:00Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}],"publist_id":"6208","volume":38,"status":"public","issue":"5","type":"journal_article","quality_controlled":"1","citation":{"ista":"Renkawitz J, Sixt MK. 2016. A Radical Break Restraining Neutrophil Migration. Developmental Cell. 38(5), 448–450.","ama":"Renkawitz J, Sixt MK. A Radical Break Restraining Neutrophil Migration. <i>Developmental Cell</i>. 2016;38(5):448-450. doi:<a href=\"https://doi.org/10.1016/j.devcel.2016.08.017\">10.1016/j.devcel.2016.08.017</a>","short":"J. Renkawitz, M.K. Sixt, Developmental Cell 38 (2016) 448–450.","chicago":"Renkawitz, Jörg, and Michael K Sixt. “A Radical Break Restraining Neutrophil Migration.” <i>Developmental Cell</i>. Cell Press, 2016. <a href=\"https://doi.org/10.1016/j.devcel.2016.08.017\">https://doi.org/10.1016/j.devcel.2016.08.017</a>.","ieee":"J. Renkawitz and M. K. Sixt, “A Radical Break Restraining Neutrophil Migration,” <i>Developmental Cell</i>, vol. 38, no. 5. Cell Press, pp. 448–450, 2016.","apa":"Renkawitz, J., &#38; Sixt, M. K. (2016). A Radical Break Restraining Neutrophil Migration. <i>Developmental Cell</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.devcel.2016.08.017\">https://doi.org/10.1016/j.devcel.2016.08.017</a>","mla":"Renkawitz, Jörg, and Michael K. Sixt. “A Radical Break Restraining Neutrophil Migration.” <i>Developmental Cell</i>, vol. 38, no. 5, Cell Press, 2016, pp. 448–50, doi:<a href=\"https://doi.org/10.1016/j.devcel.2016.08.017\">10.1016/j.devcel.2016.08.017</a>."},"date_updated":"2025-09-22T09:57:46Z","publication_status":"published","scopus_import":"1","oa_version":"None","language":[{"iso":"eng"}],"doi":"10.1016/j.devcel.2016.08.017","external_id":{"isi":["000383413000003"]},"abstract":[{"text":"When neutrophils infiltrate a site of inflammation, they have to stop at the right place to exert their effector function. In this issue of Developmental Cell, Wang et al. (2016) show that neutrophils sense reactive oxygen species via the TRPM2 channel to arrest migration at their target site. © 2016 Elsevier Inc.","lang":"eng"}],"title":"A Radical Break Restraining Neutrophil Migration","isi":1,"month":"09","publication":"Developmental Cell","page":"448 - 450","date_created":"2018-12-11T11:50:25Z","intvolume":"        38"},{"intvolume":"         6","oa":1,"date_created":"2018-12-11T11:50:27Z","publication":"Scientific Reports","month":"11","isi":1,"ddc":["579"],"abstract":[{"text":"Cellular locomotion is a central hallmark of eukaryotic life. It is governed by cell-extrinsic molecular factors, which can either emerge in the soluble phase or as immobilized, often adhesive ligands. To encode for direction, every cue must be present as a spatial or temporal gradient. Here, we developed a microfluidic chamber that allows measurement of cell migration in combined response to surface immobilized and soluble molecular gradients. As a proof of principle we study the response of dendritic cells to their major guidance cues, chemokines. The majority of data on chemokine gradient sensing is based on in vitro studies employing soluble gradients. Despite evidence suggesting that in vivo chemokines are often immobilized to sugar residues, limited information is available how cells respond to immobilized chemokines. We tracked migration of dendritic cells towards immobilized gradients of the chemokine CCL21 and varying superimposed soluble gradients of CCL19. Differential migratory patterns illustrate the potential of our setup to quantitatively study the competitive response to both types of gradients. Beyond chemokines our approach is broadly applicable to alternative systems of chemo- and haptotaxis such as cells migrating along gradients of adhesion receptor ligands vs. any soluble cue. \r\n","lang":"eng"}],"title":"A microfluidic device for measuring cell migration towards substrate bound and soluble chemokine gradients","external_id":{"isi":["000387118300001"]},"doi":"10.1038/srep36440","language":[{"iso":"eng"}],"oa_version":"Published Version","scopus_import":"1","date_updated":"2025-09-22T09:56:13Z","publication_status":"published","citation":{"apa":"Schwarz, J., Bierbaum, V., Merrin, J., Frank, T., Hauschild, R., Bollenbach, M. T., … Mehling, M. (2016). A microfluidic device for measuring cell migration towards substrate bound and soluble chemokine gradients. <i>Scientific Reports</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/srep36440\">https://doi.org/10.1038/srep36440</a>","ieee":"J. Schwarz <i>et al.</i>, “A microfluidic device for measuring cell migration towards substrate bound and soluble chemokine gradients,” <i>Scientific Reports</i>, vol. 6. Nature Publishing Group, 2016.","short":"J. Schwarz, V. Bierbaum, J. Merrin, T. Frank, R. Hauschild, M.T. Bollenbach, S. Tay, M.K. Sixt, M. Mehling, Scientific Reports 6 (2016).","chicago":"Schwarz, Jan, Veronika Bierbaum, Jack Merrin, Tino Frank, Robert Hauschild, Mark Tobias Bollenbach, Savaş Tay, Michael K Sixt, and Matthias Mehling. “A Microfluidic Device for Measuring Cell Migration towards Substrate Bound and Soluble Chemokine Gradients.” <i>Scientific Reports</i>. Nature Publishing Group, 2016. <a href=\"https://doi.org/10.1038/srep36440\">https://doi.org/10.1038/srep36440</a>.","ista":"Schwarz J, Bierbaum V, Merrin J, Frank T, Hauschild R, Bollenbach MT, Tay S, Sixt MK, Mehling M. 2016. A microfluidic device for measuring cell migration towards substrate bound and soluble chemokine gradients. Scientific Reports. 6, 36440.","ama":"Schwarz J, Bierbaum V, Merrin J, et al. A microfluidic device for measuring cell migration towards substrate bound and soluble chemokine gradients. <i>Scientific Reports</i>. 2016;6. doi:<a href=\"https://doi.org/10.1038/srep36440\">10.1038/srep36440</a>","mla":"Schwarz, Jan, et al. “A Microfluidic Device for Measuring Cell Migration towards Substrate Bound and Soluble Chemokine Gradients.” <i>Scientific Reports</i>, vol. 6, 36440, Nature Publishing Group, 2016, doi:<a href=\"https://doi.org/10.1038/srep36440\">10.1038/srep36440</a>."},"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"quality_controlled":"1","project":[{"call_identifier":"FP7","_id":"25A603A2-B435-11E9-9278-68D0E5697425","name":"Cytoskeletal force generation and force transduction of migrating leukocytes","grant_number":"281556"},{"grant_number":"Y 564-B12","call_identifier":"FWF","name":"Cytoskeletal force generation and force transduction of migrating leukocytes","_id":"25A8E5EA-B435-11E9-9278-68D0E5697425"}],"type":"journal_article","has_accepted_license":"1","article_number":"36440","ec_funded":1,"status":"public","file":[{"relation":"main_file","file_id":"4756","creator":"system","content_type":"application/pdf","file_name":"IST-2017-744-v1+1_srep36440.pdf","file_size":2353456,"date_created":"2018-12-12T10:09:32Z","date_updated":"2018-12-12T10:09:32Z","access_level":"open_access"}],"file_date_updated":"2018-12-12T10:09:32Z","volume":6,"acknowledgement":"This work was supported by the Swiss National Science Foundation (Ambizione fellowship; PZ00P3-154733 to M.M.), the Swiss Multiple Sclerosis Society (research support to M.M.), a fellowship from the Boehringer Ingelheim Fonds (BIF) to J.S., the European Research Council (grant ERC GA 281556) and a START award from the Austrian Science Foundation (FWF) to M.S. #BioimagingFacility","publist_id":"6204","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"},{"_id":"NanoFab"},{"_id":"Bio"},{"_id":"ToBo"}],"pubrep_id":"744","date_published":"2016-11-07T00:00:00Z","year":"2016","day":"07","publisher":"Nature Publishing Group","_id":"1154","article_processing_charge":"No","author":[{"full_name":"Schwarz, Jan","last_name":"Schwarz","first_name":"Jan","id":"346C1EC6-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Veronika","id":"3FD04378-F248-11E8-B48F-1D18A9856A87","last_name":"Bierbaum","full_name":"Bierbaum, Veronika"},{"orcid":"0000-0001-5145-4609","id":"4515C308-F248-11E8-B48F-1D18A9856A87","first_name":"Jack","last_name":"Merrin","full_name":"Merrin, Jack"},{"first_name":"Tino","full_name":"Frank, Tino","last_name":"Frank"},{"last_name":"Hauschild","full_name":"Hauschild, Robert","orcid":"0000-0001-9843-3522","first_name":"Robert","id":"4E01D6B4-F248-11E8-B48F-1D18A9856A87"},{"orcid":"0000-0003-4398-476X","first_name":"Mark Tobias","id":"3E6DB97A-F248-11E8-B48F-1D18A9856A87","last_name":"Bollenbach","full_name":"Bollenbach, Mark Tobias"},{"first_name":"Savaş","full_name":"Tay, Savaş","last_name":"Tay"},{"full_name":"Sixt, Michael K","last_name":"Sixt","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K","orcid":"0000-0002-6620-9179"},{"full_name":"Mehling, Matthias","last_name":"Mehling","id":"3C23B994-F248-11E8-B48F-1D18A9856A87","first_name":"Matthias","orcid":"0000-0001-8599-1226"}]},{"intvolume":"       167","month":"12","isi":1,"date_created":"2018-12-11T11:50:41Z","page":"1448 - 1449","publication":"Cell","doi":"10.1016/j.cell.2016.11.024","external_id":{"isi":["000389470500007"]},"title":"Formin’ a nuclear protection","abstract":[{"text":"In this issue of Cell, Skau et al. show that the formin FMN2 organizes a perinuclear actin cytoskeleton that protects the nucleus and its genomic content of migrating cells squeezing through small spaces.","lang":"eng"}],"date_updated":"2025-09-22T09:41:33Z","publication_status":"published","scopus_import":"1","language":[{"iso":"eng"}],"oa_version":"None","quality_controlled":"1","type":"journal_article","citation":{"short":"J. Renkawitz, M.K. Sixt, Cell 167 (2016) 1448–1449.","chicago":"Renkawitz, Jörg, and Michael K Sixt. “Formin’ a Nuclear Protection.” <i>Cell</i>. Cell Press, 2016. <a href=\"https://doi.org/10.1016/j.cell.2016.11.024\">https://doi.org/10.1016/j.cell.2016.11.024</a>.","ieee":"J. Renkawitz and M. K. Sixt, “Formin’ a nuclear protection,” <i>Cell</i>, vol. 167, no. 6. Cell Press, pp. 1448–1449, 2016.","apa":"Renkawitz, J., &#38; Sixt, M. K. (2016). Formin’ a nuclear protection. <i>Cell</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.cell.2016.11.024\">https://doi.org/10.1016/j.cell.2016.11.024</a>","ista":"Renkawitz J, Sixt MK. 2016. Formin’ a nuclear protection. Cell. 167(6), 1448–1449.","ama":"Renkawitz J, Sixt MK. Formin’ a nuclear protection. <i>Cell</i>. 2016;167(6):1448-1449. doi:<a href=\"https://doi.org/10.1016/j.cell.2016.11.024\">10.1016/j.cell.2016.11.024</a>","mla":"Renkawitz, Jörg, and Michael K. Sixt. “Formin’ a Nuclear Protection.” <i>Cell</i>, vol. 167, no. 6, Cell Press, 2016, pp. 1448–49, doi:<a href=\"https://doi.org/10.1016/j.cell.2016.11.024\">10.1016/j.cell.2016.11.024</a>."},"issue":"6","publist_id":"6149","volume":167,"status":"public","article_processing_charge":"No","_id":"1201","author":[{"orcid":"0000-0003-2856-3369","id":"3F0587C8-F248-11E8-B48F-1D18A9856A87","first_name":"Jörg","last_name":"Renkawitz","full_name":"Renkawitz, Jörg"},{"full_name":"Sixt, Michael K","last_name":"Sixt","first_name":"Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-6620-9179"}],"publisher":"Cell Press","date_published":"2016-12-01T00:00:00Z","day":"01","year":"2016","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}]},{"issue":"1","quality_controlled":"1","type":"journal_article","citation":{"mla":"Sreeramkumar, Vinatha, et al. “Efficient T-Cell Priming and Activation Requires Signaling through Prostaglandin E2 (EP) Receptors.” <i>Immunology and Cell Biology</i>, vol. 94, no. 1, Nature Publishing Group, 2016, pp. 39–51, doi:<a href=\"https://doi.org/10.1038/icb.2015.62\">10.1038/icb.2015.62</a>.","short":"V. Sreeramkumar, M. Hons, C. Punzón, J. Stein, D. Sancho, M. Fresno Forcelledo, N. Cuesta, Immunology and Cell Biology 94 (2016) 39–51.","chicago":"Sreeramkumar, Vinatha, Miroslav Hons, Carmen Punzón, Jens Stein, David Sancho, Manuel Fresno Forcelledo, and Natalia Cuesta. “Efficient T-Cell Priming and Activation Requires Signaling through Prostaglandin E2 (EP) Receptors.” <i>Immunology and Cell Biology</i>. Nature Publishing Group, 2016. <a href=\"https://doi.org/10.1038/icb.2015.62\">https://doi.org/10.1038/icb.2015.62</a>.","ieee":"V. Sreeramkumar <i>et al.</i>, “Efficient T-cell priming and activation requires signaling through prostaglandin E2 (EP) receptors,” <i>Immunology and Cell Biology</i>, vol. 94, no. 1. Nature Publishing Group, pp. 39–51, 2016.","apa":"Sreeramkumar, V., Hons, M., Punzón, C., Stein, J., Sancho, D., Fresno Forcelledo, M., &#38; Cuesta, N. (2016). Efficient T-cell priming and activation requires signaling through prostaglandin E2 (EP) receptors. <i>Immunology and Cell Biology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/icb.2015.62\">https://doi.org/10.1038/icb.2015.62</a>","ama":"Sreeramkumar V, Hons M, Punzón C, et al. Efficient T-cell priming and activation requires signaling through prostaglandin E2 (EP) receptors. <i>Immunology and Cell Biology</i>. 2016;94(1):39-51. doi:<a href=\"https://doi.org/10.1038/icb.2015.62\">10.1038/icb.2015.62</a>","ista":"Sreeramkumar V, Hons M, Punzón C, Stein J, Sancho D, Fresno Forcelledo M, Cuesta N. 2016. Efficient T-cell priming and activation requires signaling through prostaglandin E2 (EP) receptors. Immunology and Cell Biology. 94(1), 39–51."},"_id":"1217","article_processing_charge":"No","author":[{"first_name":"Vinatha","last_name":"Sreeramkumar","full_name":"Sreeramkumar, Vinatha"},{"id":"4167FE56-F248-11E8-B48F-1D18A9856A87","first_name":"Miroslav","orcid":"0000-0002-6625-3348","full_name":"Hons, Miroslav","last_name":"Hons"},{"first_name":"Carmen","last_name":"Punzón","full_name":"Punzón, Carmen"},{"first_name":"Jens","full_name":"Stein, Jens","last_name":"Stein"},{"first_name":"David","last_name":"Sancho","full_name":"Sancho, David"},{"first_name":"Manuel","last_name":"Fresno Forcelledo","full_name":"Fresno Forcelledo, Manuel"},{"full_name":"Cuesta, Natalia","last_name":"Cuesta","first_name":"Natalia"}],"publisher":"Nature Publishing Group","date_published":"2016-01-01T00:00:00Z","day":"01","year":"2016","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}],"publist_id":"6116","acknowledgement":"This manuscript has been supported by grants SAF2007-61716 and S-SAL-0159/2006 awarded by the Spanish Ministry of Science and Education and the Community of Madrid to Dr M Fresno.","volume":94,"status":"public","month":"01","isi":1,"date_created":"2018-12-11T11:50:46Z","page":"39 - 51","publication":"Immunology and Cell Biology","intvolume":"        94","date_updated":"2025-09-22T09:34:26Z","publication_status":"published","scopus_import":"1","language":[{"iso":"eng"}],"oa_version":"None","doi":"10.1038/icb.2015.62","external_id":{"isi":["000367628600005"]},"title":"Efficient T-cell priming and activation requires signaling through prostaglandin E2 (EP) receptors","abstract":[{"text":"Understanding the regulation of T-cell responses during inflammation and auto-immunity is fundamental for designing efficient therapeutic strategies against immune diseases. In this regard, prostaglandin E 2 (PGE 2) is mostly considered a myeloid-derived immunosuppressive molecule. We describe for the first time that T cells secrete PGE 2 during T-cell receptor stimulation. In addition, we show that autocrine PGE 2 signaling through EP receptors is essential for optimal CD4 + T-cell activation in vitro and in vivo, and for T helper 1 (Th1) and regulatory T cell differentiation. PGE 2 was found to provide additive co-stimulatory signaling through AKT activation. Intravital multiphoton microscopy showed that triggering EP receptors in T cells is also essential for the stability of T cell-dendritic cell (DC) interactions and Th-cell accumulation in draining lymph nodes (LNs) during inflammation. We further demonstrated that blocking EP receptors in T cells during the initial phase of collagen-induced arthritis in mice resulted in a reduction of clinical arthritis. This could be attributable to defective T-cell activation, accompanied by a decline in activated and interferon-γ-producing CD4 + Th1 cells in draining LNs. In conclusion, we prove that T lymphocytes secret picomolar concentrations of PGE 2, which in turn provide additive co-stimulatory signaling, enabling T cells to attain a favorable activation threshold. PGE 2 signaling in T cells is also required for maintaining long and stable interactions with DCs within LNs. Blockade of EP receptors in vivo impairs T-cell activation and development of T cell-mediated inflammatory responses. This may have implications in various pathophysiological settings.","lang":"eng"}]},{"oa_version":"None","language":[{"iso":"eng"}],"date_updated":"2025-09-22T08:33:40Z","publication_status":"published","scopus_import":"1","external_id":{"isi":["000389576900019"]},"title":"Focal adhesion-independent cell migration","abstract":[{"text":"Cell migration is central to a multitude of physiological processes, including embryonic development, immune surveillance, and wound healing, and deregulated migration is key to cancer dissemination. Decades of investigations have uncovered many of the molecular and physical mechanisms underlying cell migration. Together with protrusion extension and cell body retraction, adhesion to the substrate via specific focal adhesion points has long been considered an essential step in cell migration. Although this is true for cells moving on two-dimensional substrates, recent studies have demonstrated that focal adhesions are not required for cells moving in three dimensions, in which confinement is sufficient to maintain a cell in contact with its substrate. Here, we review the investigations that have led to challenging the requirement of specific adhesions for migration, discuss the physical mechanisms proposed for cell body translocation during focal adhesion-independent migration, and highlight the remaining open questions for the future.","lang":"eng"}],"doi":"10.1146/annurev-cellbio-111315-125341","publication":"Annual Review of Cell and Developmental Biology","page":"469 - 490","date_created":"2018-12-11T11:51:08Z","isi":1,"month":"10","intvolume":"        32","day":"06","year":"2016","date_published":"2016-10-06T00:00:00Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}],"_id":"1285","author":[{"full_name":"Paluch, Ewa","last_name":"Paluch","first_name":"Ewa"},{"first_name":"Irene","full_name":"Aspalter, Irene","last_name":"Aspalter"},{"last_name":"Sixt","full_name":"Sixt, Michael K","orcid":"0000-0002-6620-9179","first_name":"Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87"}],"article_processing_charge":"No","publisher":"Annual Reviews","volume":32,"status":"public","ec_funded":1,"publist_id":"6031","acknowledgement":"We would like to thank Dani Bodor for critical comments on the manuscript and Guillaume Salbreux for discussions. The authors are supported by the United Kingdom's Medical Research Council (MRC) (E.K.P. and I.M.A.; core funding to the MRC Laboratory for Molecular Cell Biology), by the European Research Council [ERC GA 311637 (E.K.P.) and ERC GA 281556 (M.S.)], and by a START award from the Austrian Science Foundation (M.S.).","citation":{"mla":"Paluch, Ewa, et al. “Focal Adhesion-Independent Cell Migration.” <i>Annual Review of Cell and Developmental Biology</i>, vol. 32, Annual Reviews, 2016, pp. 469–90, doi:<a href=\"https://doi.org/10.1146/annurev-cellbio-111315-125341\">10.1146/annurev-cellbio-111315-125341</a>.","apa":"Paluch, E., Aspalter, I., &#38; Sixt, M. K. (2016). Focal adhesion-independent cell migration. <i>Annual Review of Cell and Developmental Biology</i>. Annual Reviews. <a href=\"https://doi.org/10.1146/annurev-cellbio-111315-125341\">https://doi.org/10.1146/annurev-cellbio-111315-125341</a>","ieee":"E. Paluch, I. Aspalter, and M. K. Sixt, “Focal adhesion-independent cell migration,” <i>Annual Review of Cell and Developmental Biology</i>, vol. 32. Annual Reviews, pp. 469–490, 2016.","short":"E. Paluch, I. Aspalter, M.K. Sixt, Annual Review of Cell and Developmental Biology 32 (2016) 469–490.","chicago":"Paluch, Ewa, Irene Aspalter, and Michael K Sixt. “Focal Adhesion-Independent Cell Migration.” <i>Annual Review of Cell and Developmental Biology</i>. Annual Reviews, 2016. <a href=\"https://doi.org/10.1146/annurev-cellbio-111315-125341\">https://doi.org/10.1146/annurev-cellbio-111315-125341</a>.","ama":"Paluch E, Aspalter I, Sixt MK. Focal adhesion-independent cell migration. <i>Annual Review of Cell and Developmental Biology</i>. 2016;32:469-490. doi:<a href=\"https://doi.org/10.1146/annurev-cellbio-111315-125341\">10.1146/annurev-cellbio-111315-125341</a>","ista":"Paluch E, Aspalter I, Sixt MK. 2016. Focal adhesion-independent cell migration. Annual Review of Cell and Developmental Biology. 32, 469–490."},"type":"journal_article","quality_controlled":"1","project":[{"call_identifier":"FP7","name":"Cytoskeletal force generation and force transduction of migrating leukocytes","_id":"25A603A2-B435-11E9-9278-68D0E5697425","grant_number":"281556"},{"grant_number":"Y 564-B12","call_identifier":"FWF","_id":"25A8E5EA-B435-11E9-9278-68D0E5697425","name":"Cytoskeletal force generation and force transduction of migrating leukocytes"}]},{"status":"public","file":[{"creator":"system","file_name":"IST-2016-515-v1+1_1-s2.0-S2211124716300262-main.pdf","content_type":"application/pdf","checksum":"c98c1151d5f1e5ce1643a83d8d7f3c29","relation":"main_file","file_id":"4948","date_updated":"2020-07-14T12:44:58Z","access_level":"open_access","date_created":"2018-12-12T10:12:30Z","file_size":5489897}],"volume":14,"file_date_updated":"2020-07-14T12:44:58Z","publist_id":"5697","department":[{"_id":"MiSi"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","pubrep_id":"515","date_published":"2016-02-23T00:00:00Z","year":"2016","day":"23","publisher":"Cell Press","_id":"1490","article_processing_charge":"No","author":[{"last_name":"Russo","full_name":"Russo, Erica","first_name":"Erica"},{"first_name":"Alvaro","full_name":"Teijeira, Alvaro","last_name":"Teijeira"},{"orcid":"0000-0001-7829-3518","first_name":"Kari","id":"368EE576-F248-11E8-B48F-1D18A9856A87","last_name":"Vaahtomeri","full_name":"Vaahtomeri, Kari"},{"last_name":"Willrodt","full_name":"Willrodt, Ann","first_name":"Ann"},{"full_name":"Bloch, Joël","last_name":"Bloch","first_name":"Joël"},{"last_name":"Nitschké","full_name":"Nitschké, Maximilian","first_name":"Maximilian"},{"full_name":"Santambrogio, Laura","last_name":"Santambrogio","first_name":"Laura"},{"full_name":"Kerjaschki, Dontscho","last_name":"Kerjaschki","first_name":"Dontscho"},{"full_name":"Sixt, Michael K","last_name":"Sixt","first_name":"Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-6620-9179"},{"last_name":"Halin","full_name":"Halin, Cornelia","first_name":"Cornelia"}],"citation":{"mla":"Russo, Erica, et al. “Intralymphatic CCL21 Promotes Tissue Egress of Dendritic Cells through Afferent Lymphatic Vessels.” <i>Cell Reports</i>, vol. 14, no. 7, Cell Press, 2016, pp. 1723–34, doi:<a href=\"https://doi.org/10.1016/j.celrep.2016.01.048\">10.1016/j.celrep.2016.01.048</a>.","chicago":"Russo, Erica, Alvaro Teijeira, Kari Vaahtomeri, Ann Willrodt, Joël Bloch, Maximilian Nitschké, Laura Santambrogio, Dontscho Kerjaschki, Michael K Sixt, and Cornelia Halin. “Intralymphatic CCL21 Promotes Tissue Egress of Dendritic Cells through Afferent Lymphatic Vessels.” <i>Cell Reports</i>. Cell Press, 2016. <a href=\"https://doi.org/10.1016/j.celrep.2016.01.048\">https://doi.org/10.1016/j.celrep.2016.01.048</a>.","short":"E. Russo, A. Teijeira, K. Vaahtomeri, A. Willrodt, J. Bloch, M. Nitschké, L. Santambrogio, D. Kerjaschki, M.K. Sixt, C. Halin, Cell Reports 14 (2016) 1723–1734.","apa":"Russo, E., Teijeira, A., Vaahtomeri, K., Willrodt, A., Bloch, J., Nitschké, M., … Halin, C. (2016). Intralymphatic CCL21 promotes tissue egress of dendritic cells through afferent lymphatic vessels. <i>Cell Reports</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.celrep.2016.01.048\">https://doi.org/10.1016/j.celrep.2016.01.048</a>","ieee":"E. Russo <i>et al.</i>, “Intralymphatic CCL21 promotes tissue egress of dendritic cells through afferent lymphatic vessels,” <i>Cell Reports</i>, vol. 14, no. 7. Cell Press, pp. 1723–1734, 2016.","ista":"Russo E, Teijeira A, Vaahtomeri K, Willrodt A, Bloch J, Nitschké M, Santambrogio L, Kerjaschki D, Sixt MK, Halin C. 2016. Intralymphatic CCL21 promotes tissue egress of dendritic cells through afferent lymphatic vessels. Cell Reports. 14(7), 1723–1734.","ama":"Russo E, Teijeira A, Vaahtomeri K, et al. Intralymphatic CCL21 promotes tissue egress of dendritic cells through afferent lymphatic vessels. <i>Cell Reports</i>. 2016;14(7):1723-1734. doi:<a href=\"https://doi.org/10.1016/j.celrep.2016.01.048\">10.1016/j.celrep.2016.01.048</a>"},"tmp":{"short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode"},"quality_controlled":"1","type":"journal_article","has_accepted_license":"1","issue":"7","title":"Intralymphatic CCL21 promotes tissue egress of dendritic cells through afferent lymphatic vessels","abstract":[{"lang":"eng","text":"To induce adaptive immunity, dendritic cells (DCs) migrate through afferent lymphatic vessels (LVs) to draining lymph nodes (dLNs). This process occurs in several consecutive steps. Upon entry into lymphatic capillaries, DCs first actively crawl into downstream collecting vessels. From there, they are next passively and rapidly transported to the dLN by lymph flow. Here, we describe a role for the chemokine CCL21 in intralymphatic DC crawling. Performing time-lapse imaging in murine skin, we found that blockade of CCL21-but not the absence of lymph flow-completely abolished DC migration from capillaries toward collecting vessels and reduced the ability of intralymphatic DCs to emigrate from skin. Moreover, we found that in vitro low laminar flow established a CCL21 gradient along lymphatic endothelial monolayers, thereby inducing downstream-directed DC migration. These findings reveal a role for intralymphatic CCL21 in promoting DC trafficking to dLNs, through the formation of a flow-induced gradient."}],"external_id":{"isi":["000370970200016"]},"doi":"10.1016/j.celrep.2016.01.048","language":[{"iso":"eng"}],"oa_version":"Published Version","scopus_import":"1","date_updated":"2025-09-18T11:16:44Z","publication_status":"published","intvolume":"        14","oa":1,"date_created":"2018-12-11T11:52:19Z","publication":"Cell Reports","page":"1723 - 1734","month":"02","ddc":["570"],"isi":1},{"main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6400263","open_access":"1"}],"issue":"12","pmid":1,"quality_controlled":"1","type":"journal_article","article_type":"original","citation":{"ama":"Salzer E, Çaǧdaş D, Hons M, et al. RASGRP1 deficiency causes immunodeficiency with impaired cytoskeletal dynamics. <i>Nature Immunology</i>. 2016;17(12):1352-1360. doi:<a href=\"https://doi.org/10.1038/ni.3575\">10.1038/ni.3575</a>","ista":"Salzer E, Çaǧdaş D, Hons M, Mace E, Garncarz W, Petronczki O, Platzer R, Pfajfer L, Bilic I, Ban S, Willmann K, Mukherjee M, Supper V, Hsu H, Banerjee P, Sinha P, Mcclanahan F, Zlabinger G, Pickl W, Gribben J, Stockinger H, Bennett K, Huppa J, Dupré L, Sanal Ö, Jäger U, Sixt MK, Tezcan I, Orange J, Boztug K. 2016. RASGRP1 deficiency causes immunodeficiency with impaired cytoskeletal dynamics. Nature Immunology. 17(12), 1352–1360.","apa":"Salzer, E., Çaǧdaş, D., Hons, M., Mace, E., Garncarz, W., Petronczki, O., … Boztug, K. (2016). RASGRP1 deficiency causes immunodeficiency with impaired cytoskeletal dynamics. <i>Nature Immunology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/ni.3575\">https://doi.org/10.1038/ni.3575</a>","ieee":"E. Salzer <i>et al.</i>, “RASGRP1 deficiency causes immunodeficiency with impaired cytoskeletal dynamics,” <i>Nature Immunology</i>, vol. 17, no. 12. Nature Publishing Group, pp. 1352–1360, 2016.","short":"E. Salzer, D. Çaǧdaş, M. Hons, E. Mace, W. Garncarz, O. Petronczki, R. Platzer, L. Pfajfer, I. Bilic, S. Ban, K. Willmann, M. Mukherjee, V. Supper, H. Hsu, P. Banerjee, P. Sinha, F. Mcclanahan, G. Zlabinger, W. Pickl, J. Gribben, H. Stockinger, K. Bennett, J. Huppa, L. Dupré, Ö. Sanal, U. Jäger, M.K. Sixt, I. Tezcan, J. Orange, K. Boztug, Nature Immunology 17 (2016) 1352–1360.","chicago":"Salzer, Elisabeth, Deniz Çaǧdaş, Miroslav Hons, Emily Mace, Wojciech Garncarz, Oezlem Petronczki, René Platzer, et al. “RASGRP1 Deficiency Causes Immunodeficiency with Impaired Cytoskeletal Dynamics.” <i>Nature Immunology</i>. Nature Publishing Group, 2016. <a href=\"https://doi.org/10.1038/ni.3575\">https://doi.org/10.1038/ni.3575</a>.","mla":"Salzer, Elisabeth, et al. “RASGRP1 Deficiency Causes Immunodeficiency with Impaired Cytoskeletal Dynamics.” <i>Nature Immunology</i>, vol. 17, no. 12, Nature Publishing Group, 2016, pp. 1352–60, doi:<a href=\"https://doi.org/10.1038/ni.3575\">10.1038/ni.3575</a>."},"article_processing_charge":"No","_id":"1137","author":[{"first_name":"Elisabeth","full_name":"Salzer, Elisabeth","last_name":"Salzer"},{"first_name":"Deniz","full_name":"Çaǧdaş, Deniz","last_name":"Çaǧdaş"},{"orcid":"0000-0002-6625-3348","first_name":"Miroslav","id":"4167FE56-F248-11E8-B48F-1D18A9856A87","last_name":"Hons","full_name":"Hons, Miroslav"},{"first_name":"Emily","last_name":"Mace","full_name":"Mace, Emily"},{"first_name":"Wojciech","last_name":"Garncarz","full_name":"Garncarz, Wojciech"},{"last_name":"Petronczki","full_name":"Petronczki, Oezlem","first_name":"Oezlem"},{"full_name":"Platzer, René","last_name":"Platzer","first_name":"René"},{"full_name":"Pfajfer, Laurène","last_name":"Pfajfer","first_name":"Laurène"},{"first_name":"Ivan","full_name":"Bilic, Ivan","last_name":"Bilic"},{"first_name":"Sol","full_name":"Ban, Sol","last_name":"Ban"},{"last_name":"Willmann","full_name":"Willmann, Katharina","first_name":"Katharina"},{"first_name":"Malini","full_name":"Mukherjee, Malini","last_name":"Mukherjee"},{"first_name":"Verena","full_name":"Supper, Verena","last_name":"Supper"},{"last_name":"Hsu","full_name":"Hsu, Hsiangting","first_name":"Hsiangting"},{"first_name":"Pinaki","full_name":"Banerjee, Pinaki","last_name":"Banerjee"},{"first_name":"Papiya","full_name":"Sinha, Papiya","last_name":"Sinha"},{"full_name":"Mcclanahan, Fabienne","last_name":"Mcclanahan","first_name":"Fabienne"},{"full_name":"Zlabinger, Gerhard","last_name":"Zlabinger","first_name":"Gerhard"},{"last_name":"Pickl","full_name":"Pickl, Winfried","first_name":"Winfried"},{"first_name":"John","last_name":"Gribben","full_name":"Gribben, John"},{"last_name":"Stockinger","full_name":"Stockinger, Hannes","first_name":"Hannes"},{"full_name":"Bennett, Keiryn","last_name":"Bennett","first_name":"Keiryn"},{"first_name":"Johannes","last_name":"Huppa","full_name":"Huppa, Johannes"},{"first_name":"Loï̈C","last_name":"Dupré","full_name":"Dupré, Loï̈C"},{"last_name":"Sanal","full_name":"Sanal, Özden","first_name":"Özden"},{"first_name":"Ulrich","last_name":"Jäger","full_name":"Jäger, Ulrich"},{"id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","first_name":"Michael K","orcid":"0000-0002-6620-9179","full_name":"Sixt, Michael K","last_name":"Sixt"},{"full_name":"Tezcan, Ilhan","last_name":"Tezcan","first_name":"Ilhan"},{"last_name":"Orange","full_name":"Orange, Jordan","first_name":"Jordan"},{"first_name":"Kaan","last_name":"Boztug","full_name":"Boztug, Kaan"}],"publisher":"Nature Publishing Group","date_published":"2016-12-01T00:00:00Z","year":"2016","day":"01","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","department":[{"_id":"MiSi"}],"publist_id":"6221","volume":17,"status":"public","month":"12","isi":1,"date_created":"2018-12-11T11:50:21Z","publication":"Nature Immunology","page":"1352 - 1360","oa":1,"intvolume":"        17","publication_status":"published","date_updated":"2025-09-22T14:13:22Z","scopus_import":"1","language":[{"iso":"eng"}],"oa_version":"Submitted Version","doi":"10.1038/ni.3575","external_id":{"isi":["000388056400005"],"pmid":["27776107"]},"abstract":[{"text":"RASGRP1 is an important guanine nucleotide exchange factor and activator of the RAS-MAPK pathway following T cell antigen receptor (TCR) signaling. The consequences of RASGRP1 mutations in humans are unknown. In a patient with recurrent bacterial and viral infections, born to healthy consanguineous parents, we used homozygosity mapping and exome sequencing to identify a biallelic stop-gain variant in RASGRP1. This variant segregated perfectly with the disease and has not been reported in genetic databases. RASGRP1 deficiency was associated in T cells and B cells with decreased phosphorylation of the extracellular-signal-regulated serine kinase ERK, which was restored following expression of wild-type RASGRP1. RASGRP1 deficiency also resulted in defective proliferation, activation and motility of T cells and B cells. RASGRP1-deficient natural killer (NK) cells exhibited impaired cytotoxicity with defective granule convergence and actin accumulation. Interaction proteomics identified the dynein light chain DYNLL1 as interacting with RASGRP1, which links RASGRP1 to cytoskeletal dynamics. RASGRP1-deficient cells showed decreased activation of the GTPase RhoA. Treatment with lenalidomide increased RhoA activity and reversed the migration and activation defects of RASGRP1-deficient lymphocytes.","lang":"eng"}],"title":"RASGRP1 deficiency causes immunodeficiency with impaired cytoskeletal dynamics"},{"main_file_link":[{"url":"https://ora.ox.ac.uk/objects/uuid:f53a464e-1e5b-4f08-a7d8-b6749b852b9d","open_access":"1"}],"issue":"12","citation":{"mla":"Martins, Rui, et al. “Heme Drives Hemolysis-Induced Susceptibility to Infection via Disruption of Phagocyte Functions.” <i>Nature Immunology</i>, vol. 17, no. 12, Nature Publishing Group, 2016, pp. 1361–72, doi:<a href=\"https://doi.org/10.1038/ni.3590\">10.1038/ni.3590</a>.","apa":"Martins, R., Maier, J., Gorki, A., Huber, K., Sharif, O., Starkl, P., … Knapp, S. (2016). Heme drives hemolysis-induced susceptibility to infection via disruption of phagocyte functions. <i>Nature Immunology</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/ni.3590\">https://doi.org/10.1038/ni.3590</a>","ieee":"R. Martins <i>et al.</i>, “Heme drives hemolysis-induced susceptibility to infection via disruption of phagocyte functions,” <i>Nature Immunology</i>, vol. 17, no. 12. Nature Publishing Group, pp. 1361–1372, 2016.","chicago":"Martins, Rui, Julia Maier, Anna Gorki, Kilian Huber, Omar Sharif, Philipp Starkl, Simona Saluzzo, et al. “Heme Drives Hemolysis-Induced Susceptibility to Infection via Disruption of Phagocyte Functions.” <i>Nature Immunology</i>. Nature Publishing Group, 2016. <a href=\"https://doi.org/10.1038/ni.3590\">https://doi.org/10.1038/ni.3590</a>.","short":"R. Martins, J. Maier, A. Gorki, K. Huber, O. Sharif, P. Starkl, S. Saluzzo, F. Quattrone, R. Gawish, K. Lakovits, M. Aichinger, B. Radic Sarikas, C. Lardeau, A. Hladik, A. Korosec, M. Brown, K. Vaahtomeri, M. Duggan, D. Kerjaschki, H. Esterbauer, J. Colinge, S. Eisenbarth, T. Decker, K. Bennett, S. Kubicek, M.K. Sixt, G. Superti Furga, S. Knapp, Nature Immunology 17 (2016) 1361–1372.","ista":"Martins R, Maier J, Gorki A, Huber K, Sharif O, Starkl P, Saluzzo S, Quattrone F, Gawish R, Lakovits K, Aichinger M, Radic Sarikas B, Lardeau C, Hladik A, Korosec A, Brown M, Vaahtomeri K, Duggan M, Kerjaschki D, Esterbauer H, Colinge J, Eisenbarth S, Decker T, Bennett K, Kubicek S, Sixt MK, Superti Furga G, Knapp S. 2016. Heme drives hemolysis-induced susceptibility to infection via disruption of phagocyte functions. Nature Immunology. 17(12), 1361–1372.","ama":"Martins R, Maier J, Gorki A, et al. Heme drives hemolysis-induced susceptibility to infection via disruption of phagocyte functions. <i>Nature Immunology</i>. 2016;17(12):1361-1372. doi:<a href=\"https://doi.org/10.1038/ni.3590\">10.1038/ni.3590</a>"},"quality_controlled":"1","type":"journal_article","date_published":"2016-12-01T00:00:00Z","year":"2016","day":"01","department":[{"_id":"MiSi"},{"_id":"PeJo"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","author":[{"first_name":"Rui","last_name":"Martins","full_name":"Martins, Rui"},{"first_name":"Julia","full_name":"Maier, Julia","last_name":"Maier"},{"first_name":"Anna","last_name":"Gorki","full_name":"Gorki, Anna"},{"full_name":"Huber, Kilian","last_name":"Huber","first_name":"Kilian"},{"first_name":"Omar","full_name":"Sharif, Omar","last_name":"Sharif"},{"first_name":"Philipp","full_name":"Starkl, Philipp","last_name":"Starkl"},{"first_name":"Simona","full_name":"Saluzzo, Simona","last_name":"Saluzzo"},{"last_name":"Quattrone","full_name":"Quattrone, Federica","first_name":"Federica"},{"full_name":"Gawish, Riem","last_name":"Gawish","first_name":"Riem"},{"first_name":"Karin","full_name":"Lakovits, Karin","last_name":"Lakovits"},{"last_name":"Aichinger","full_name":"Aichinger, Michael","first_name":"Michael"},{"first_name":"Branka","full_name":"Radic Sarikas, Branka","last_name":"Radic Sarikas"},{"first_name":"Charles","full_name":"Lardeau, Charles","last_name":"Lardeau"},{"last_name":"Hladik","full_name":"Hladik, Anastasiya","first_name":"Anastasiya"},{"full_name":"Korosec, Ana","last_name":"Korosec","first_name":"Ana"},{"id":"3DAB9AFC-F248-11E8-B48F-1D18A9856A87","first_name":"Markus","last_name":"Brown","full_name":"Brown, Markus"},{"id":"368EE576-F248-11E8-B48F-1D18A9856A87","first_name":"Kari","orcid":"0000-0001-7829-3518","full_name":"Vaahtomeri, Kari","last_name":"Vaahtomeri"},{"id":"2EDEA62C-F248-11E8-B48F-1D18A9856A87","first_name":"Michelle","last_name":"Duggan","full_name":"Duggan, Michelle"},{"first_name":"Dontscho","full_name":"Kerjaschki, Dontscho","last_name":"Kerjaschki"},{"first_name":"Harald","full_name":"Esterbauer, Harald","last_name":"Esterbauer"},{"first_name":"Jacques","full_name":"Colinge, Jacques","last_name":"Colinge"},{"first_name":"Stephanie","last_name":"Eisenbarth","full_name":"Eisenbarth, Stephanie"},{"full_name":"Decker, Thomas","last_name":"Decker","first_name":"Thomas"},{"last_name":"Bennett","full_name":"Bennett, Keiryn","first_name":"Keiryn"},{"full_name":"Kubicek, Stefan","last_name":"Kubicek","first_name":"Stefan"},{"full_name":"Sixt, Michael K","last_name":"Sixt","first_name":"Michael K","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-6620-9179"},{"first_name":"Giulio","last_name":"Superti Furga","full_name":"Superti Furga, Giulio"},{"last_name":"Knapp","full_name":"Knapp, Sylvia","first_name":"Sylvia"}],"_id":"1142","article_processing_charge":"No","publisher":"Nature Publishing Group","volume":17,"status":"public","publist_id":"6216","acknowledgement":"Y. Fukui (Medical Institute of Bioregulation, Kyushu University) and J. Stein (Theodor Kocher Institute, University of Bern) are acknowledged for providing the DOCK8 deficient bone marrow. and H. Häcker (St. Judes Children's Research Hospital) for providing the ERHBD-HoxB8-encoding retroviral construct. pSpCas9(BB)-2a-Puro (PX459) was a gift from F. Zhang (Massachusetts Institute of Technology) (Addgene plasmid # 48139) and pGRG36 was a gift from N. Craig (Johns Hopkins University School of Medicine) (Addgene plasmid # 16666). LifeAct-GFP-encoding retrovirus was kindly provided by A. Leithner (Institute of Science and Technology Austria). pSIM8 and TKC E. coli were gifts from D.L. Court (Center for Cancer Research, National Cancer Institute). We acknowledge M. Gröger and S. Rauscher for excellent technical support (Core imaging facility, Medical University of Vienna). We thank D.P. Barlow and L.R. Cheever for critical reading of the manuscript. This work was supported by the Austrian Academy of Sciences, the Science Fund of the Austrian National Bank (14107) and the Austrian Science Fund FWF (I1620-B22) in the Infect-ERA framework (to S.Knapp).","date_created":"2018-12-11T11:50:22Z","page":"1361 - 1372","publication":"Nature Immunology","month":"12","isi":1,"intvolume":"        17","oa":1,"language":[{"iso":"eng"}],"oa_version":"Submitted Version","publication_status":"published","date_updated":"2025-09-22T14:10:50Z","scopus_import":"1","external_id":{"isi":["000388056400006"]},"title":"Heme drives hemolysis-induced susceptibility to infection via disruption of phagocyte functions","abstract":[{"lang":"eng","text":"Hemolysis drives susceptibility to bacterial infections and predicts poor outcome from sepsis. These detrimental effects are commonly considered to be a consequence of heme-iron serving as a nutrient for bacteria. We employed a Gram-negative sepsis model and found that elevated heme levels impaired the control of bacterial proliferation independently of heme-iron acquisition by pathogens. Heme strongly inhibited phagocytosis and the migration of human and mouse phagocytes by disrupting actin cytoskeletal dynamics via activation of the GTP-binding Rho family protein Cdc42 by the guanine nucleotide exchange factor DOCK8. A chemical screening approach revealed that quinine effectively prevented heme effects on the cytoskeleton, restored phagocytosis and improved survival in sepsis. These mechanistic insights provide potential therapeutic targets for patients with sepsis or hemolytic disorders."}],"doi":"10.1038/ni.3590"}]