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dc.contributor.authorRognoni, Lorenz
dc.contributor.authorStigler, Johannes
dc.contributor.authorPelz, Benjamin
dc.contributor.authorYlänne, Jari
dc.contributor.authorRief, Matthias
dc.date.accessioned2016-06-13T10:59:10Z
dc.date.available2016-06-13T10:59:10Z
dc.date.issued2012
dc.identifier.citationRognoni, L., Stigler, J., Pelz, B., Ylänne, J., & Rief, M. (2012). Dynamic force sensing of filamin revealed in single-molecule experiments. <em>Proceedings of the National Academy of Sciences of the United States of America</em>, 109 (48), 19679-19684. <a href="http://dx.doi.org/10.1073/pnas.1211274109">doi:10.1073/pnas.1211274109</a> Retrieved from <a href="http://www.pnas.org/content/109/48/19679.long">http://www.pnas.org/content/109/48/19679.long</a>
dc.identifier.otherTUTKAID_54620
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/50280
dc.description.abstractMechanical forces are important signals for cell response and development, but detailed molecular mechanisms of force sensing are largely unexplored. The cytoskeletal protein filamin is a key connecting element between the cytoskeleton and transmembrane complexes such as integrins or the von Willebrand receptor glycoprotein Ib. Here, we show using single-molecule mechanical measurements that the recently reported Ig domain pair 20–21 of human filamin A acts as an autoinhibited force-activatable mechanosensor. We developed a mechanical single-molecule competition assay that allows online observation of binding events of target peptides in solution to the strained domain pair. We find that filamin force sensing is a highly dynamic process occurring in rapid equilibrium that increases the affinity to the target peptides by up to a factor of 17 between 2 and 5 pN. The equilibrium mechanism we find here can offer a general scheme for cellular force sensing.
dc.publisherStanford University's Highwire Press
dc.relation.ispartofseriesProceedings of the National Academy of Sciences of the United States of America
dc.relation.urihttp://www.pnas.org/content/109/48/19679.long
dc.subject.otherfilamin
dc.subject.otheractin-binding protein
dc.subject.otheroptical tweezer
dc.subject.othermechanosensing
dc.titleDynamic force sensing of filamin revealed in single-molecule experiments
dc.identifier.urnURN:NBN:fi:jyu-201301241109
dc.contributor.laitosBio- ja ympäristötieteiden laitos
dc.contributor.oppiaineSolu- ja molekyylibiologia
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2013-01-24T04:30:07Z
dc.type.coarjournal article
dc.description.reviewstatuspeerReviewed
dc.format.pagerange19679-19684
dc.relation.issn1091-6490
dc.relation.numberinseries48
dc.relation.volume109
dc.type.versionacceptedVersion
dc.rights.copyright© National Academy of Sciences, 2012. This is a final draft version of an article whose final and definitive form has been published by NAS. Published in this repository with the kind permission of the publisher.
dc.rights.accesslevelopenAccessfi
dc.relation.doi10.1073/pnas.1211274109


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