Journal
CELLULAR AND MOLECULAR BIOENGINEERING
Volume 2, Issue 1, Pages 28-38Publisher
SPRINGER
DOI: 10.1007/s12195-009-0048-8
Keywords
F-actin; Filamin; Single molecule; Network
Funding
- NIGMS [GM076689]
- NSF Career [0643745]
- Nicholas Hobson Wheeles, Jr. Fellowship,
- W. M. Keck Foundation
- Westaway Research Fund
- Singapore-MIT Alliance for Research and Technology
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0643745] Funding Source: National Science Foundation
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Actin cytoskeleton has long been a focus of attention due to its biological significance and unique rheological properties. Although F-actin networks have been extensively studied experimentally and several theoretical models proposed, the detailed molecular interactions between actin binding proteins (ABPs) and actin. laments that regulate network behavior remain unclear. Here, using an in vitro assay that allows direct measurements on the bond between one actin cross-linking protein and two actin. laments, we demonstrate force-induced unbinding and unfolding of. lamin. The critical forces prove to be similar, 70 +/- 23 pN for unbinding and 57 +/- 19 pN for unfolding, suggesting that both are important mechanisms governing cytoskeletal rheology. We also obtain the mechanical response of a cross-linked F-actin network to an optically trapped microbead and observe abrupt transitions implying rupture or unfolding of cross-links. These measurements are interpreted with the aid of a computational simulation of the experiment to provide greater insight into physical mechanisms.
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