Objective To investigate the mechanism and molecular structural basis of tension-regulated interaction between ICAP1 and β1 integrin. Methods Based on the crystal structure data of the ICAP1/β1 integrin cytoplasmic tail complex (PDB ID: 4DX9), tensile molecular dynamics simulations were conducted to observe and analyze the effects of tension loading on β1 integrin on the structure and binding affinity of the ICAP1/β1 integrin complex. Results Tension modulates the dissociation of the ICAP1/β1 integrin complex bidirectionally by inducing local conformational changes at the binding interface. It initially increases and then decreases the binding affinity of β1 integrin for ICAP1, with the threshold point occurring at 10 pN. The main tension-sensitive residue interactions are primarily located among ARG_¹⁴⁰-THR_⁷⁸⁹, MET_¹⁴¹-THR_⁷⁸⁹, and ASP_¹⁴⁵-SER_⁷⁸⁵.Conclusion As the tension applied to the cytoplasmic tail of β1 integrin increases, conformational changes at the binding interface lead to an initial enhancement followed by a reduction in the inhibitory effect of ICAP1 on β1 integrin activation. The tension threshold is observed at 10 pN, indicating that integrin activation induced by force requires sufficient mechanical stimulus strength.