Focal adhesions (FAs) are specialized sites of adhesion between cells and the extracellular matrix (ECM), consisting of aggregated ECM receptors (integrins) and actin filaments. The assembly of FAs is regulated by the GTP-binding protein Rho, which stimulates contractility and generates isometric tension. This tension leads to the bundling of actin filaments and the aggregation of integrins, activating focal adhesion kinase (FAK) and forming a multicomponent signaling complex. Integrins, the major transmembrane components of FAs, are classified into several families based on their α and β subunits. The cytoplasmic domains of integrins are crucial for FA formation, with the β subunit cytoplasmic domain responsible for targeting integrins to FAs. Rho is a key regulator of FA formation, and its activation is influenced by various factors such as integrin clustering and ligand occupancy. The regulation of contractility, particularly by myosin light chain (MLC) phosphorylation, is also discussed, highlighting the role of MLCK and other regulatory proteins. The interaction between Rho and phosphatidylinositol-4,5-bisphosphate (PIP₂) is highlighted, as PIP₂ levels are elevated in response to adhesion and promote FA formation. Additionally, Rho activates serine/threonine kinases, including ROKα and p160ROCK, which are potential downstream targets.Focal adhesions (FAs) are specialized sites of adhesion between cells and the extracellular matrix (ECM), consisting of aggregated ECM receptors (integrins) and actin filaments. The assembly of FAs is regulated by the GTP-binding protein Rho, which stimulates contractility and generates isometric tension. This tension leads to the bundling of actin filaments and the aggregation of integrins, activating focal adhesion kinase (FAK) and forming a multicomponent signaling complex. Integrins, the major transmembrane components of FAs, are classified into several families based on their α and β subunits. The cytoplasmic domains of integrins are crucial for FA formation, with the β subunit cytoplasmic domain responsible for targeting integrins to FAs. Rho is a key regulator of FA formation, and its activation is influenced by various factors such as integrin clustering and ligand occupancy. The regulation of contractility, particularly by myosin light chain (MLC) phosphorylation, is also discussed, highlighting the role of MLCK and other regulatory proteins. The interaction between Rho and phosphatidylinositol-4,5-bisphosphate (PIP₂) is highlighted, as PIP₂ levels are elevated in response to adhesion and promote FA formation. Additionally, Rho activates serine/threonine kinases, including ROKα and p160ROCK, which are potential downstream targets.