Vinculin, a key regulator of focal adhesions (FAs), controls integrin dynamics and clustering, and links FAs to the actin cytoskeleton. Using vinculin mutants, the study separates the vinculin head and tail regions into distinct functional domains. The head region, which includes the N-terminal 258 amino acids (D1 domain), regulates integrin clustering and FA growth by interacting with talin. This interaction leads to an increase in integrin residency time in FAs. In contrast, the tail region, which includes the C-terminal 192 amino acids (vinT), is responsible for the functional link of FAs to the actin network. The study proposes a new model where the head region forms a tight complex with talin and α5β1 integrin, while the tail region links this complex to actin filaments. This model explains how vinculin orchestrates FA formation and turnover.Vinculin, a key regulator of focal adhesions (FAs), controls integrin dynamics and clustering, and links FAs to the actin cytoskeleton. Using vinculin mutants, the study separates the vinculin head and tail regions into distinct functional domains. The head region, which includes the N-terminal 258 amino acids (D1 domain), regulates integrin clustering and FA growth by interacting with talin. This interaction leads to an increase in integrin residency time in FAs. In contrast, the tail region, which includes the C-terminal 192 amino acids (vinT), is responsible for the functional link of FAs to the actin network. The study proposes a new model where the head region forms a tight complex with talin and α5β1 integrin, while the tail region links this complex to actin filaments. This model explains how vinculin orchestrates FA formation and turnover.