Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation
Holes in endothelial barriers, called transendothelial cell macroapertures (TEMs), are predicted to be limited by line tension of unknown origin. Here the authors identify an actomyosin cable encircling TEMs and establish a role for ezrin in stabilising F-actin bundles, allowing their crosslinking b...
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Nature Publishing Group
2017-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms15839 |
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doaj-b124a0879bef45a0aa24bea545ed4ff22021-05-11T07:45:18ZengNature Publishing GroupNature Communications2041-17232017-06-018111410.1038/ncomms15839Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formationCaroline Stefani0David Gonzalez-Rodriguez1Yosuke Senju2Anne Doye3Nadia Efimova4Sébastien Janel5Justine Lipuma6Meng Chen Tsai7Daniel Hamaoui8Madhavi P. Maddugoda9Olivier Cochet-Escartin10Coline Prévost11Frank Lafont12Tatyana Svitkina13Pekka Lappalainen14Patricia Bassereau15Emmanuel Lemichez16Department of microbial toxins in host-pathogen interactions, INSERM, U1065, Université de Nice-Sophia Antipolis, Centre Méditerranéen de Médecine Moléculaire (C3M)LCP-A2MC, Institut Jean Barriol, Université de LorraineProgram in Cell and Molecular Biology, Institute of Biotechnology, P.O. Box 56, University of HelsinkiDepartment of microbial toxins in host-pathogen interactions, INSERM, U1065, Université de Nice-Sophia Antipolis, Centre Méditerranéen de Médecine Moléculaire (C3M)Department of Biology, University of PennsylvaniaMultiscale Physics-Biology-Chemistry and Cancer, Cellular Microbiology and Physics of Infection Group, Center for Infection and Immunity of Lille, CNRS UMR8204, INSERM U1019, Institut Pasteur de Lille, Centre Hospitalier Régional de Lille, Université de LilleDepartment of microbial toxins in host-pathogen interactions, INSERM, U1065, Université de Nice-Sophia Antipolis, Centre Méditerranéen de Médecine Moléculaire (C3M)Department of microbial toxins in host-pathogen interactions, INSERM, U1065, Université de Nice-Sophia Antipolis, Centre Méditerranéen de Médecine Moléculaire (C3M)Department of microbial toxins in host-pathogen interactions, INSERM, U1065, Université de Nice-Sophia Antipolis, Centre Méditerranéen de Médecine Moléculaire (C3M)Department of microbial toxins in host-pathogen interactions, INSERM, U1065, Université de Nice-Sophia Antipolis, Centre Méditerranéen de Médecine Moléculaire (C3M)Multiscale Physics-Biology-Chemistry and Cancer, Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS, UMR168Multiscale Physics-Biology-Chemistry and Cancer, Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS, UMR168Multiscale Physics-Biology-Chemistry and Cancer, Cellular Microbiology and Physics of Infection Group, Center for Infection and Immunity of Lille, CNRS UMR8204, INSERM U1019, Institut Pasteur de Lille, Centre Hospitalier Régional de Lille, Université de LilleDepartment of Biology, University of PennsylvaniaProgram in Cell and Molecular Biology, Institute of Biotechnology, P.O. Box 56, University of HelsinkiMultiscale Physics-Biology-Chemistry and Cancer, Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS, UMR168Department of microbial toxins in host-pathogen interactions, INSERM, U1065, Université de Nice-Sophia Antipolis, Centre Méditerranéen de Médecine Moléculaire (C3M)Holes in endothelial barriers, called transendothelial cell macroapertures (TEMs), are predicted to be limited by line tension of unknown origin. Here the authors identify an actomyosin cable encircling TEMs and establish a role for ezrin in stabilising F-actin bundles, allowing their crosslinking by non-muscle myosin IIa.https://doi.org/10.1038/ncomms15839 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Caroline Stefani David Gonzalez-Rodriguez Yosuke Senju Anne Doye Nadia Efimova Sébastien Janel Justine Lipuma Meng Chen Tsai Daniel Hamaoui Madhavi P. Maddugoda Olivier Cochet-Escartin Coline Prévost Frank Lafont Tatyana Svitkina Pekka Lappalainen Patricia Bassereau Emmanuel Lemichez |
| spellingShingle |
Caroline Stefani David Gonzalez-Rodriguez Yosuke Senju Anne Doye Nadia Efimova Sébastien Janel Justine Lipuma Meng Chen Tsai Daniel Hamaoui Madhavi P. Maddugoda Olivier Cochet-Escartin Coline Prévost Frank Lafont Tatyana Svitkina Pekka Lappalainen Patricia Bassereau Emmanuel Lemichez Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation Nature Communications |
| author_facet |
Caroline Stefani David Gonzalez-Rodriguez Yosuke Senju Anne Doye Nadia Efimova Sébastien Janel Justine Lipuma Meng Chen Tsai Daniel Hamaoui Madhavi P. Maddugoda Olivier Cochet-Escartin Coline Prévost Frank Lafont Tatyana Svitkina Pekka Lappalainen Patricia Bassereau Emmanuel Lemichez |
| author_sort |
Caroline Stefani |
| title |
Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation |
| title_short |
Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation |
| title_full |
Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation |
| title_fullStr |
Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation |
| title_full_unstemmed |
Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation |
| title_sort |
ezrin enhances line tension along transcellular tunnel edges via nmiia driven actomyosin cable formation |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2017-06-01 |
| description |
Holes in endothelial barriers, called transendothelial cell macroapertures (TEMs), are predicted to be limited by line tension of unknown origin. Here the authors identify an actomyosin cable encircling TEMs and establish a role for ezrin in stabilising F-actin bundles, allowing their crosslinking by non-muscle myosin IIa. |
| url |
https://doi.org/10.1038/ncomms15839 |
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