期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 48, 页码 19679-19684出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1211274109
关键词
optical tweezers; mechanosensing
资金
- Deutsche Forschungsgemeinschaft [FOR 1352, Sonderforschungsbereich 863 B7]
- Academy of Finland [138327]
- Institute for Advanced Study of Technische Universitat Munchen
- Academy of Finland (AKA) [138327, 138327] Funding Source: Academy of Finland (AKA)
Mechanical 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.
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