Abstract
[Formula: see text]-catenin is an adhesion protein located at the cadherin-based cell–cell adherens junction. [Formula: see text]-catenin cross-links [Formula: see text]-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 [Formula: see text]-catenin modulation domains under different loading rates from which the unfolding distance of M2 and M3 domains is determined to be 5–7[Formula: see text]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.
Highlights
Adherens junction between cells plays an important role in many biological processes, such as cell morphogenesis, cancer cell metastasis, wound healing, and embryonic development.[1]
Extracellular domain of transmembrane protein E-cadherin binds with E-cadherin on adjacent cells to link cells together, while cytoplasmic domain of E-cadherin links to actinber cytoskeleton through cross-linker proteins of -catenin and -catenin.[2]
The catenins function as cross-linkers, and regulate the growth of adhesion site in a force-dependent manner.3 -catenin binds cytoplasmic domain of E-cadherin to form a protein complex
Summary
Adherens junction between cells plays an important role in many biological processes, such as cell morphogenesis, cancer cell metastasis, wound healing, and embryonic development.[1]. The catenins function as cross-linkers, and regulate the growth of adhesion site in a force-dependent manner.3 -catenin binds cytoplasmic domain of E-cadherin to form a protein complex. In vitro experiment found that E-cadherin -catenin- -catenin is the minimal protein complex to combine with actinber.[6] But the interaction between this protein complex and actinber is quite weak.
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