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.
- 出版日期2019-1
- 单位厦门大学