001     10586
005     20200402205851.0
024 7 _ |2 pmid
|a pmid:21386436
024 7 _ |2 DOI
|a 10.1088/0953-8984/22/19/194109
024 7 _ |2 WOS
|a WOS:000277033100012
037 _ _ |a PreJuSER-10586
041 _ _ |a eng
082 _ _ |a 530
084 _ _ |2 WoS
|a Physics, Condensed Matter
100 1 _ |a Kirchenbüchler, D.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB84090
245 _ _ |a Substrate, focal adhesion and actin filaments: A mechanical unit with a weak spot for mechanosensitive proteins
260 _ _ |a Bristol
|b IOP Publ.
|c 2010
300 _ _ |a 194109
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Journal of Physics: Condensed Matter
|x 0953-8984
|0 3703
|v 22
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Mechanosensing 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.
536 _ _ |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK505
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Actin Cytoskeleton: physiology
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Cell Adhesion: physiology
650 _ 2 |2 MeSH
|a Cells, Cultured
650 _ 2 |2 MeSH
|a Fibroblasts: physiology
650 _ 2 |2 MeSH
|a Intracellular Signaling Peptides and Proteins: physiology
650 _ 2 |2 MeSH
|a Mechanotransduction, Cellular: physiology
650 _ 2 |2 MeSH
|a Rats
650 _ 2 |2 MeSH
|a Rats, Wistar
650 _ 7 |0 0
|2 NLM Chemicals
|a Intracellular Signaling Peptides and Proteins
650 _ 7 |a J
|2 WoSType
700 1 _ |a Born, S.
|b 1
|u FZJ
|0 P:(DE-Juel1)161241
700 1 _ |a Kirchgeßner, N.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB8902
700 1 _ |a Houben, S.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB87855
700 1 _ |a Hoffmann, B.
|b 4
|u FZJ
|0 P:(DE-Juel1)VDB27696
700 1 _ |a Merkel, R.
|b 5
|u FZJ
|0 P:(DE-Juel1)128833
773 _ _ |a 10.1088/0953-8984/22/19/194109
|g Vol. 22, p. 194109
|p 194109
|q 22<194109
|0 PERI:(DE-600)1472968-4
|t Journal of physics / Condensed matter
|v 22
|y 2010
|x 0953-8984
856 7 _ |u http://dx.doi.org/10.1088/0953-8984/22/19/194109
909 C O |o oai:juser.fz-juelich.de:10586
|p VDB
913 1 _ |k P45
|v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|l Biologische Informationsverarbeitung
|b Schlüsseltechnologien
|0 G:(DE-Juel1)FUEK505
|x 0
913 2 _ |a DE-HGF
|b Key Technologies
|l BioSoft Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences
|1 G:(DE-HGF)POF3-550
|0 G:(DE-HGF)POF3-552
|2 G:(DE-HGF)POF3-500
|v Engineering Cell Function
|x 0
914 1 _ |y 2010
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k IBN-4
|l Biomechanik
|d 31.12.2010
|g IBN
|0 I:(DE-Juel1)VDB802
|x 0
970 _ _ |a VDB:(DE-Juel1)120977
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980 _ _ |a journal
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980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBI-2-20200312
981 _ _ |a I:(DE-Juel1)ICS-7-20110106


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