Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/32456
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dc.contributor.authorBate, N.-
dc.contributor.authorMargadant, F.-
dc.contributor.authorChew, L. L.-
dc.contributor.authorHu, X.-
dc.contributor.authorYu, H.-
dc.contributor.authorZhang, X.-
dc.contributor.authorSheetz, M.-
dc.date.accessioned2015-06-30T11:43:02Z-
dc.date.available2015-06-30T11:43:02Z-
dc.date.issued2011-12-20-
dc.identifier.citationPLoS Biology, 2011, 9(12), e1001223en
dc.identifier.issn1544-9173-
dc.identifier.urihttp://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.1001223en
dc.identifier.urihttp://hdl.handle.net/2381/32456-
dc.description.abstractMechanotransduction is a critical function for cells, in terms of cell viability, shaping of tissues, and cellular behavior. In vitro, cellular level forces can stretch adhesion proteins that link extracellular matrix to the actin cytoskeleton exposing hidden binding sites. However, there is no evidence that in vivo forces produce significant in vivo stretching to cause domain unfolding. We now report that the adhesion protein, talin, is repeatedly stretched by 100–350 nm in vivo by myosin contraction of actin filaments. Using a functional EGFP-N-Talin1-C-mCherry to measure the length of single talin molecules, we observed that the C-terminal mCherry was normally displaced in the direction of actin flow by 90 to >250 nm from N-EGFP but only by 50–60 nm (talin's length in vitro) after myosin inhibition. Individual talin molecules transiently stretched and relaxed. Peripheral, multimolecular adhesions had green outside and red proximal edges. They also exhibited transient, myosin-dependent stretching of 50–350 nm for 6–16 s; however, expression of the talin-binding head of vinculin increased stretching to about 400 nm and suppressed dynamics. We suggest that rearward moving actin filaments bind, stretch, and release talin in multiple, stochastic stick-slip cycles and that multiple vinculin binding and release cycles integrate pulling on matrices into biochemical signals.en
dc.language.isoenen
dc.publisherPublic Library of Scienceen
dc.relation.urihttp://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.1001223-
dc.rights© 2011 Margadant et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.subjectFocal adhesionsen
dc.subjectSignal filteringen
dc.subjectActinsen
dc.subjectMyosinsen
dc.subjectFluorescence imagingen
dc.subjectExtracellular matrix proteinsen
dc.subjectMotor proteinsen
dc.subjectMuscle contractionen
dc.titleMechanotransduction In Vivo by Repeated Talin Stretch-Relaxation Events Depends upon Vinculinen
dc.typeJournal Articleen
dc.identifier.doi10.1371/journal.pbio.1001223-
dc.identifier.eissn1545-7885-
dc.description.statusPeer-revieweden
dc.description.versionPublisher Versionen
dc.type.subtypeArticle-
pubs.organisational-group/Organisationen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGYen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/School of Biological Sciencesen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/School of Biological Sciences/Department of Biochemistryen
Appears in Collections:Published Articles, Dept. of Biochemistry

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