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1.
Cell Rep ; 21(10): 2714-2723, 2017 Dec 05.
Article in English | MEDLINE | ID: mdl-29212020

ABSTRACT

α-Actinins, a family of critical cytoskeletal actin-binding proteins that usually exist as anti-parallel dimers, play crucial roles in organizing the framework of the cytoskeleton through crosslinking the actin filaments, as well as in focal adhesion maturation. However, the molecular mechanisms underlying its functions are unclear. Here, by mechanical manipulation of single human α-actinin 1 using magnetic tweezers, we determined the mechanical stability and kinetics of the functional domains in α-actinin 1. Moreover, we identified the force-dependence of vinculin binding to α-actinin 1, with the demonstration that force is required to expose the high-affinity binding site for vinculin binding. Further, a role of the α-actinin 1 as molecular shock absorber for the cytoskeleton network is revealed. Our results provide a comprehensive analysis of the force-dependent stability and interactions of α-actinin 1, which sheds important light on the molecular mechanisms underlying its mechanotransmission and mechanosensing functions.


Subject(s)
Actinin/metabolism , Actinin/chemistry , Cytoskeleton/metabolism , Humans , Kinetics , Magnetite Nanoparticles/chemistry , Mechanotransduction, Cellular/genetics , Mechanotransduction, Cellular/physiology , Vinculin/chemistry
2.
Nano Lett ; 16(7): 4062-8, 2016 07 13.
Article in English | MEDLINE | ID: mdl-27210030

ABSTRACT

The dimeric focal adhesion protein talin contains up to 22 cryptic vinculin binding sites that are exposed by unfolding. Using a novel method to monitor the in situ dynamics of the talin dimer stretch, we find that in contrast to several prevalent talin dimer models the integrin-binding talin N-termini are separated by 162 ± 44 nm on average whereas as expected the C-terminal dimerization domains colocalize and are mobile. Using vinculin tagged by DHFR-TMP Atto655 label, we found that optimal vinculin and vinculin head binding occurred when talin was stretched to 180 nm, while the controls did not bind to talin. Surprisingly, multiple vinculins bound within a single second in narrowly localized regions of the talin rod during stretching. We suggest that talin stretches as an antiparallel dimer and that activates vinculin binding in a cooperative manner, consistent with the stabilization of folded talin by other binding proteins.

3.
Scanning ; 27(1): 1-7, 2005.
Article in English | MEDLINE | ID: mdl-15712751

ABSTRACT

We present a vector implementation for nonlinear filters that allows an efficient execution on graphics processing units. These filters are popular to suppress shot noise arising in low light conditions. Having them available at the end of the visualization stage makes this setup particularly suitable for handling the postprocessing stages for light microscopy. Without vector acceleration, these filters constitute a bottleneck since real time or frequent update volume rendering has become available on desktop workstations. Even simple averaging operations can push the overall system's performance noticeably below the original frame rate.

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