Force-dependent unfolding and folding dynamics of protein alpha-catenin modulation domains

作者:Li, Xueping; Zhai, Weili; Guo, Zilong; Chen, Hu*
来源:Journal of Innovative Optical Health Sciences, 2019, 12(1): 1841001.
DOI:10.1142/S1793545818410018

摘要

alpha-catenin is an adhesion protein located at the cadherin-based cell-cell adherens junction. alpha-catenin cross-links beta-catenin and actin fiber in the adhesion protein complex, and plays an important role in the formation and modulation of cell-cell adhesion. The central modulation domains can be unfolded to expose binding site of vinculin when stretching force is applied. Here, we studied the force-induced unfolding dynamics of alpha-catenin modulation domains under different loading rates from which the unfolding distance of M2 and M3 domains is determined to be 5-7 nm, and an unfolding intermediate state is identified. We also found that the folding process of M1-M3 domains goes through different pathways with cooperativity.

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