α-catenin is an adhesion protein located at the cadherin-based cell–cell adherens junction. α-catenin cross-links β-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 α-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.