Paxillin: A Hub for Mechano-Transduction from the β3 Integrin-Talin-Kindlin Axis

Focal adhesions are specialized integrin-dependent adhesion complexes, which ensure cell anchoring to the extracellular matrix. Focal adhesions also function as mechano-signaling platforms by perceiving and integrating diverse physical and (bio)chemical cues of their microenvironment, and by transducing them into intracellular signaling for the control of cell behavior. The fundamental biological mechanism of creating intracellular signaling in response to changes in tensional forces appears to be tightly linked to paxillin recruitment and binding to focal adhesions. Interestingly, the tension-dependent nature of the paxillin binding to adhesions, combined with its scaffolding function, suggests a major role of this protein in integrating multiple signals from the microenvironment, and accordingly activating diverse molecular responses. This minireview offers an overview of the molecular bases of the mechano-sensitivity and mechano-signaling capacity of core focal adhesion proteins, and highlights the role of paxillin as a key component of the mechano-transducing machinery based on the interaction of cells to substrates activating the beta 3 integrin-talin1-kindlin.

Automated summary

Focal adhesions are cell structures that anchor cells to the extracellular matrix and also play a role in mechanosignaling by integrating physical and chemical cues from the microenvironment. Paxillin, a protein involved in focal adhesion formation and scaffolding, appears to have a key role in integrating multiple signals and activating various molecular responses from the microenvironment. This minireview provides an overview of the molecular mechanisms underlying the mechanosensitivity and mechanosignaling capacity of core focal adhesion proteins, with a focus on the role of paxillin.