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- W2053128269 abstract "Filamin A (FLNa) is one of the most ubiquitous actin binding proteins that cross-link actin filaments. The protein is a v-shaped homodimer. Each monomer consists of twenty-four β-sheet “rod-like” domains which separate the actin binding domain at the N-terminus from the C-terminus at the dimerization site. The rod-like domains are divided by two unstructured “hinge” sequences between repeats 15 and 16 and repeats 23 and 24. While it has been reported that these hinge sequences play a key role in determining the nonlinear elastic response of stressed actin networks, how the hinge segment elicits such changes in network elasticity remains unknown. To elucidate this mechanism, we measure the torsional dynamics of single FLNa molecules in real-time by using high-resolution, fluorescence microscopy. Using a native-like single-molecule assay consisting of the complex formed by a surface-bound actin filament cross-linked to a freely-rotating actin filament by FLNa we are able to track the instantaneous angle between the cross-linked filaments as the cross-linked filament undergoes a thermally-driven rotational motion. By estimating the torsional stiffness of both wildtype and hingeless FLNa isoforms, the role of the hinge sequence in determining the torsional rigidity of FLNa is inferred. Both hinged and hingeless FLNa form cross-links with comparable near-acute angles. Moreover, the torsional dynamics of each cross-link can be distinctly categorized by using this strategy to image the molecular interactions present in each cross-link. This work may illuminate the molecular origins of the nonlinear elasticity observed in FLNa-cross-linked F-actin networks. Support from the Singapore-MIT Alliance for Research and Technology and the NSF Career Award (0643745) are gratefully acknowledged." @default.
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- W2053128269 date "2010-01-01" @default.
- W2053128269 modified "2023-09-27" @default.
- W2053128269 title "Measurement of Filamin a Torsion In-Singulo" @default.
- W2053128269 doi "https://doi.org/10.1016/j.bpj.2009.12.835" @default.
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