Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/62018
Título : Mechanical properties of β-catenin revealed by single-molecule experiments
Autor : Valbuena, A., Vera, A.M., Oroz, J., Menéndez, Margarita, Carrión-Vázquez, Mariano Sixto
Fecha de publicación : 2012
Editor: Biophysical Society
Resumen: β-catenin is a central component of the adaptor complex that links cadherins to the actin cytoskeleton in adherens junctions and thus, it is a good candidate to sense and transmit mechanical forces to trigger specific changes inside the cell. To fully understand its molecular physiology, we must first investigate its mechanical role in mechanotransduction within the cadherin system. We have studied the mechanical response of β-catenin to stretching using single-molecule force spectroscopy and molecular dynamics. Unlike most proteins analyzed to date, which have a fixed mechanical unfolding pathway, the β-catenin armadillo repeat region (ARM) displays low mechanostability and multiple alternative unfolding pathways that seem to be modulated by its unstructured termini. These results are supported by steered molecular dynamics simulations, which also predict its mechanical stabilization and unfolding pathway restrictions when the contiguous α-helix of the C-terminal unstructured region is included. Furthermore, simulations of the ARM/E-cadherin cytosolic tail complex emulating the most probable stress geometry occurring in vivo show a mechanical stabilization of the interaction whose magnitude correlates with the length of the stretch of the cadherin cytosolic tail that is in contact with the ARM region. © 2012 Biophysical Society.
URI : http://hdl.handle.net/10261/62018
Identificadores: doi: 10.1016/j.bpj.2012.07.051
issn: 0006-3495
Citación : Biophysical Journal 103: 1744-1752 (2012)
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