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10.1038/srep17225 http://scihub22266oqcxt.onion/10.1038/srep17225 C4661603!4661603!26611125     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26611125&cmd=llinks): Failed to open stream: HTTP request failed! 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VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the ?-catenin-vinculin module |pdf=|usr=}}{{26611125}} gab.com Text VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the -catenin-vinculin module JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26611125 #FOAvip Mechanical forces are integrated at cadherin-based adhesion complexes to regulate morphology and strength of cell-cell junctions and organization of associated F-actin. A central mechanosensor at the cadherin complex is ?-catenin, whose stretching recruits vinculin to regulate adhesion strength. The identity of the F-actin regulating signals that are also activated by mechanical forces at cadherin-based junctions has remained elusive. Here we identify the actin-regulators VASP, zyxin and TES as members of punctate, tensile cadherin-based junctions called Focal Adherens Junctions (FAJ) and show that they display mechanosensitive recruitment similar to that of vinculin. However, this recruitment is not altered by destroying or over-activating the ?-catenin/vinculin module. Structured Illumination Microscopy (SIM) indicates that these tension sensitive proteins concentrate at locations within FAJs that are distinct from the core cadherin complex proteins. Furthermore, localization studies using mutated versions of VASP and zyxin indicate that these two proteins require binding to each other in order to localize to the FAJs. We conclude that there are multiple force sensitive modules present at the FAJ that are activated at distinct locations along the cadherin-F-actin axis and regulate specific aspects of junction dynamics. Twit Text FOAVip VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the -catenin-vinculin module ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26611125 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26611125 #FOAvip English Wikipedia <ref>{{Cite pmid|26611125}}</ref> VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the ?-catenin-vinculin module #MMPMID26611125 Oldenburg J; van der Krogt G; Twiss F; Bongaarts A; Habani Y; Slotman JA; Houtsmuller A; Huveneers S; de Rooij J Sci Rep 2015[]; 5 (ä): ä PMID26611125show ga Mechanical forces are integrated at cadherin-based adhesion complexes to regulate morphology and strength of cell-cell junctions and organization of associated F-actin. A central mechanosensor at the cadherin complex is ?-catenin, whose stretching recruits vinculin to regulate adhesion strength. The identity of the F-actin regulating signals that are also activated by mechanical forces at cadherin-based junctions has remained elusive. Here we identify the actin-regulators VASP, zyxin and TES as members of punctate, tensile cadherin-based junctions called Focal Adherens Junctions (FAJ) and show that they display mechanosensitive recruitment similar to that of vinculin. However, this recruitment is not altered by destroying or over-activating the ?-catenin/vinculin module. Structured Illumination Microscopy (SIM) indicates that these tension sensitive proteins concentrate at locations within FAJs that are distinct from the core cadherin complex proteins. Furthermore, localization studies using mutated versions of VASP and zyxin indicate that these two proteins require binding to each other in order to localize to the FAJs. We conclude that there are multiple force sensitive modules present at the FAJ that are activated at distinct locations along the cadherin-F-actin axis and regulate specific aspects of junction dynamics. äVASP, zyxin and TES are tension-dependent members of Focal Adherens Ju(epmc).pdf DeepDyve Pubget Overpricing