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000840578 1001_ $$0P:(DE-HGF)0$$aRinger, Pia$$b0
000840578 245__ $$aMultiplexing molecular tension sensors reveals piconewton force gradient across talin-1
000840578 260__ $$aLondon [u.a.] Nature Publishing Group$$c2017
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000840578 520__ $$aFörster resonance energy transfer (FRET)-based tension sensor modules (TSMs) are available for investigating how distinct proteins bear mechanical forces in cells. Yet, forces in the single piconewton (pN) regime remain difficult to resolve, and tools for multiplexed tension sensing are lacking. Here, we report the generation and calibration of a genetically encoded, FRET-based biosensor called FL-TSM, which is characterized by a near-digital force response and increased sensitivity at 3–5 pN. In addition, we present a method allowing the simultaneous evaluation of coexpressed tension sensor constructs using two-color fluorescence lifetime microscopy. Finally, we introduce a procedure to calculate the fraction of mechanically engaged molecules within cells. Application of these techniques to new talin biosensors reveals an intramolecular tension gradient across talin-1 that is established upon integrin-mediated cell adhesion. The tension gradient is actomyosin- and vinculin-dependent and sensitive to the rigidity of the extracellular environment.
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000840578 7001_ $$0P:(DE-HGF)0$$aWeißl, Andreas$$b1
000840578 7001_ $$0P:(DE-HGF)0$$aCost, Anna-Lena$$b2
000840578 7001_ $$0P:(DE-HGF)0$$aFreikamp, Andrea$$b3
000840578 7001_ $$0P:(DE-Juel1)171489$$aSabass, Benedikt$$b4
000840578 7001_ $$0P:(DE-HGF)0$$aMehlich, Alexander$$b5
000840578 7001_ $$0P:(DE-HGF)0$$aTramier, Marc$$b6
000840578 7001_ $$0P:(DE-HGF)0$$aRief, Matthias$$b7
000840578 7001_ $$00000-0003-0118-9231$$aGrashoff, Carsten$$b8$$eCorresponding author
000840578 773__ $$0PERI:(DE-600)2163081-1$$a10.1038/nmeth.4431$$gVol. 14, no. 11, p. 1090 - 1096$$n11$$p1090 - 1096$$tNature methods$$v14$$x1548-7105$$y2017
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