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

Chunmei Lv, Xiang Gao, Wenfei Li, Bo Xue, Meng Qin, Leslie D. Burtnick, Hao Zhou, Yi Cao (), Robert C. Robinson () and Wei Wang ()
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Chunmei Lv: National Laboratory of Solid State Microstructure, Nanjing University
Xiang Gao: National Laboratory of Solid State Microstructure, Nanjing University
Wenfei Li: National Laboratory of Solid State Microstructure, Nanjing University
Bo Xue: Institute of Molecular and Cell Biology, A*STAR
Meng Qin: National Laboratory of Solid State Microstructure, Nanjing University
Leslie D. Burtnick: Life Sciences Institute, University of British Columbia
Hao Zhou: State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University
Yi Cao: National Laboratory of Solid State Microstructure, Nanjing University
Robert C. Robinson: Institute of Molecular and Cell Biology, A*STAR
Wei Wang: National Laboratory of Solid State Microstructure, Nanjing University

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms5623

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