Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin

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Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin
Title:
Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin
Journal Title:
Nature Communications
Keywords:
Publication Date:
07 August 2014
Citation:
Nature Communications 5, Article number: 4623
Abstract:
Force is increasingly recognized as an important element in controlling biological processes. Forces can deform native protein conformations leading to protein-specific effects. Protein–protein binding affinities may be decreased, or novel protein–protein interaction sites may be revealed, on mechanically stressing one or more components. Here we demonstrate that the calcium-binding affinity of the sixth domain of the actin-binding protein ​gelsolin (G6) can be enhanced by mechanical force. Our kinetic model suggests that the calcium-binding affinity of G6 increases exponentially with force, up to the point of G6 unfolding. This implies that ​gelsolin may be activated at lower calcium ion levels when subjected to tensile forces. The demonstration that cation–protein binding affinities can be force-dependent provides a new understanding of the complex behaviour of cation-regulated proteins in stressful cellular environments, such as those found in the cytoskeleton-rich leading edge and at cell adhesions.
License type:
http://creativecommons.org/licenses/by-nc-sa/4.0/
Funding Info:
Description:
ISSN:
2041-1723
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