000010586 001__ 10586
000010586 005__ 20200402205851.0
000010586 0247_ $$2pmid$$apmid:21386436
000010586 0247_ $$2DOI$$a10.1088/0953-8984/22/19/194109
000010586 0247_ $$2WOS$$aWOS:000277033100012
000010586 037__ $$aPreJuSER-10586
000010586 041__ $$aeng
000010586 082__ $$a530
000010586 084__ $$2WoS$$aPhysics, Condensed Matter
000010586 1001_ $$0P:(DE-Juel1)VDB84090$$aKirchenbüchler, D.$$b0$$uFZJ
000010586 245__ $$aSubstrate, focal adhesion and actin filaments: A mechanical unit with a weak spot for mechanosensitive proteins
000010586 260__ $$aBristol$$bIOP Publ.$$c2010
000010586 300__ $$a194109
000010586 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000010586 3367_ $$2DataCite$$aOutput Types/Journal article
000010586 3367_ $$00$$2EndNote$$aJournal Article
000010586 3367_ $$2BibTeX$$aARTICLE
000010586 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000010586 3367_ $$2DRIVER$$aarticle
000010586 440_0 $$03703$$aJournal of Physics: Condensed Matter$$v22$$x0953-8984
000010586 500__ $$aRecord converted from VDB: 12.11.2012
000010586 520__ $$aMechanosensing is a vital prerequisite for dynamic remodeling of focal adhesions and cytoskeletal structures upon substrate deformation. For example, tissue formation, directed cell orientation or cell differentiation are regulated by such mechanosensing processes. Focal adhesions and the actin cytoskeleton are believed to be involved in these processes, but where mechanosensing molecules are located and how elastic substrate, focal adhesions and the cytoskeleton couple with each other upon substrate deformation still remains obscure. To approach these questions we have developed a sensitive method to apply defined spatially decaying deformation fields to cells cultivated on ultrasoft elastic substrates and to accurately quantify the resulting displacements of the actin cytoskeleton, focal adhesions, as well as the substrate. Displacement fields were recorded in live cell microscopy by tracking either signals from fluorescent proteins or marker particles in the substrate. As model cell type we used myofibroblasts. These cells are characterized by highly stable adhesion and force generating structures but are still able to detect mechanical signals with high sensitivity. We found a rigid connection between substrate and focal adhesions. Furthermore, stress fibers were found to be barely extendable almost over their whole lengths. Plastic deformation took place only at the very ends of actin filaments close to focal adhesions. As a result, this area became elongated without extension of existing actin filaments by polymerization. Both ends of the stress fibers were mechanically coupled with detectable plastic deformations on either site. Interestingly, traction force dependent substrate deformation fields remained mostly unaffected even when stress fiber elongations were released. These data argue for a location of mechanosensing proteins at the ends of actin stress fibers and describe, except for these domains, the whole system to be relatively rigid for tensile strain with a mechanical coupling between the front and rear end of a cell.
000010586 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
000010586 588__ $$aDataset connected to Web of Science, Pubmed
000010586 650_2 $$2MeSH$$aActin Cytoskeleton: physiology
000010586 650_2 $$2MeSH$$aAnimals
000010586 650_2 $$2MeSH$$aCell Adhesion: physiology
000010586 650_2 $$2MeSH$$aCells, Cultured
000010586 650_2 $$2MeSH$$aFibroblasts: physiology
000010586 650_2 $$2MeSH$$aIntracellular Signaling Peptides and Proteins: physiology
000010586 650_2 $$2MeSH$$aMechanotransduction, Cellular: physiology
000010586 650_2 $$2MeSH$$aRats
000010586 650_2 $$2MeSH$$aRats, Wistar
000010586 650_7 $$00$$2NLM Chemicals$$aIntracellular Signaling Peptides and Proteins
000010586 650_7 $$2WoSType$$aJ
000010586 7001_ $$0P:(DE-Juel1)161241$$aBorn, S.$$b1$$uFZJ
000010586 7001_ $$0P:(DE-Juel1)VDB8902$$aKirchgeßner, N.$$b2$$uFZJ
000010586 7001_ $$0P:(DE-Juel1)VDB87855$$aHouben, S.$$b3$$uFZJ
000010586 7001_ $$0P:(DE-Juel1)VDB27696$$aHoffmann, B.$$b4$$uFZJ
000010586 7001_ $$0P:(DE-Juel1)128833$$aMerkel, R.$$b5$$uFZJ
000010586 773__ $$0PERI:(DE-600)1472968-4$$a10.1088/0953-8984/22/19/194109$$gVol. 22, p. 194109$$p194109$$q22<194109$$tJournal of physics / Condensed matter$$v22$$x0953-8984$$y2010
000010586 8567_ $$uhttp://dx.doi.org/10.1088/0953-8984/22/19/194109
000010586 909CO $$ooai:juser.fz-juelich.de:10586$$pVDB
000010586 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x0
000010586 9132_ $$0G:(DE-HGF)POF3-552$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft  Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vEngineering Cell Function$$x0
000010586 9141_ $$y2010
000010586 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000010586 9201_ $$0I:(DE-Juel1)VDB802$$d31.12.2010$$gIBN$$kIBN-4$$lBiomechanik$$x0
000010586 970__ $$aVDB:(DE-Juel1)120977
000010586 980__ $$aVDB
000010586 980__ $$aConvertedRecord
000010586 980__ $$ajournal
000010586 980__ $$aI:(DE-Juel1)ICS-7-20110106
000010586 980__ $$aUNRESTRICTED
000010586 981__ $$aI:(DE-Juel1)IBI-2-20200312
000010586 981__ $$aI:(DE-Juel1)ICS-7-20110106