Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation

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Stefani , C , Gonzalez-Rodriguez , D , Senju , Y , Doye , A , Efimova , N , Janel , S , Lipuma , J , Tsai , M C , Hamaoui , D , Maddugoda , M P , Cochet-Escartin , O , Prevost , C , Lafont , F , Svitkina , T , Lappalainen , P , Bassereau , P & Lemichez , E 2017 , ' Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation ' , Nature Communications , vol. 8 , 15839 . https://doi.org/10.1038/ncomms15839

Title: Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation
Author: Stefani, Caroline; Gonzalez-Rodriguez, David; Senju, Yosuke; Doye, Anne; Efimova, Nadia; Janel, Sebastien; Lipuma, Justine; Tsai, Meng Chen; Hamaoui, Daniel; Maddugoda, Madhavi P.; Cochet-Escartin, Olivier; Prevost, Coline; Lafont, Frank; Svitkina, Tatyana; Lappalainen, Pekka; Bassereau, Patricia; Lemichez, Emmanuel
Other contributor: University of Helsinki, Institute of Biotechnology
University of Helsinki, Institute of Biotechnology

Date: 2017-06-23
Language: eng
Number of pages: 14
Belongs to series: Nature Communications
ISSN: 2041-1723
DOI: https://doi.org/10.1038/ncomms15839
URI: http://hdl.handle.net/10138/232769
Abstract: Transendothelial cell macroaperture (TEM) tunnels control endothelium barrier function and are triggered by several toxins from pathogenic bacteria that provoke vascular leakage. Cellular dewetting theory predicted that a line tension of uncharacterized origin works at TEM boundaries to limit their widening. Here, by conducting high-resolution microscopy approaches we unveil the presence of an actomyosin cable encircling TEMs. We develop a theoretical cellular dewetting framework to interpret TEM physical parameters that are quantitatively determined by laser ablation experiments. This establishes the critical role of ezrin and non-muscle myosin II (NMII) in the progressive implementation of line tension. Mechanistically, fluorescence-recovery-after-photobleaching experiments point for the upstream role of ezrin in stabilizing actin filaments at the edges of TEMs, thereby favouring their crosslinking by NMIIa. Collectively, our findings ascribe to ezrin and NMIIa a critical function of enhancing line tension at the cell boundary surrounding the TEMs by promoting the formation of an actomyosin ring.
Subject: MYOSIN-II
PHENOTYPIC HETEROGENEITY
STAPHYLOCOCCUS-AUREUS
ACTIN POLYMERIZATION
EPITHELIAL CLOSURE
STRESS FIBERS
F-ACTIN
MIGRATION
DYNAMICS
CELLS
1182 Biochemistry, cell and molecular biology
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