Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms7111
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dc.titleMechanics of epithelial closure over non-adherent environments
dc.contributor.authorVedula, S.R.K
dc.contributor.authorPeyret, G
dc.contributor.authorCheddadi, I
dc.contributor.authorChen, T
dc.contributor.authorBrugués, A
dc.contributor.authorHirata, H
dc.contributor.authorLopez-Menendez, H
dc.contributor.authorToyama, Y
dc.contributor.authorNeves De Almeida, L
dc.contributor.authorTrepat, X
dc.contributor.authorLim, C.T
dc.contributor.authorLadoux, B
dc.date.accessioned2020-09-10T01:58:29Z
dc.date.available2020-09-10T01:58:29Z
dc.date.issued2015
dc.identifier.citationVedula, S.R.K, Peyret, G, Cheddadi, I, Chen, T, Brugués, A, Hirata, H, Lopez-Menendez, H, Toyama, Y, Neves De Almeida, L, Trepat, X, Lim, C.T, Ladoux, B (2015). Mechanics of epithelial closure over non-adherent environments. Nature Communications 6 : 6111. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms7111
dc.identifier.issn20411723
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/175517
dc.description.abstractThe closure of gaps within epithelia is crucial to maintain its integrity during biological processes such as wound healing and gastrulation. Depending on the distribution of extracellular matrix, gap closure occurs through assembly of multicellular actin-based contractile cables or protrusive activity of border cells into the gap. Here we show that the supracellular actomyosin contractility of cells near the gap edge exerts sufficient tension on the surrounding tissue to promote closure of non-adherent gaps. Using traction force microscopy, we observe that cell-generated forces on the substrate at the gap edge first point away from the centre of the gap and then increase in the radial direction pointing into the gap as closure proceeds. Combining with numerical simulations, we show that the increase in force relies less on localized purse-string contractility and more on large-scale remodelling of the suspended tissue around the gap. Our results provide a framework for understanding the assembly and the mechanics of cellular contractility at the tissue level. © 2015 Macmillan Publishers Limited. All rights reserved.
dc.publisherNature Publishing Group
dc.sourceUnpaywall 20200831
dc.subjectmyosin adenosine triphosphatase
dc.subjectactin
dc.subjectmyosin adenosine triphosphatase
dc.subjectArticle
dc.subjectcell proliferation
dc.subjectcontrolled study
dc.subjectepithelium cell
dc.subjectforce
dc.subjecthuman
dc.subjecthuman cell
dc.subjectkeratinocyte
dc.subjectmechanics
dc.subjectmicroscopy
dc.subjectmolecular model
dc.subjectsimulation
dc.subjecttension
dc.subjecttissue level
dc.subjecttraction force microscopy
dc.subjectactin filament
dc.subjectanimal
dc.subjectatomic force microscopy
dc.subjectcell adhesion
dc.subjectchemistry
dc.subjectcomputer simulation
dc.subjectconfocal microscopy
dc.subjectdog
dc.subjectepithelium
dc.subjectextracellular matrix
dc.subjectMDCK cell line
dc.subjectmetabolism
dc.subjecttheoretical model
dc.subjecttumor cell line
dc.subjectActin Cytoskeleton
dc.subjectActins
dc.subjectActomyosin
dc.subjectAnimals
dc.subjectCell Adhesion
dc.subjectCell Line, Tumor
dc.subjectCell Proliferation
dc.subjectComputer Simulation
dc.subjectDogs
dc.subjectEpithelium
dc.subjectExtracellular Matrix
dc.subjectHumans
dc.subjectMadin Darby Canine Kidney Cells
dc.subjectMicroscopy, Atomic Force
dc.subjectMicroscopy, Confocal
dc.subjectModels, Theoretical
dc.typeArticle
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.departmentBIOENGINEERING
dc.contributor.departmentBIOLOGY (NU)
dc.description.doi10.1038/ncomms7111
dc.description.sourcetitleNature Communications
dc.description.volume6
dc.description.page6111
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