Skip to Main Content


The integrin family of adhesion receptors provides a dynamic, tightly regulated link between extracellular matrix (or cellular counter-receptors) and intracellular cytoskeletal and signaling networks, enabling cells to sense and respond to their chemical and physical environment. Integrin-mediated cell adhesion is thus a key regulator of cell morphology, proliferation, migration, and differentiation, and controls tissue morphogenesis, angiogenesis, wound healing, hemostasis and the immune response. Perturbation of normal integrin adhesion and signaling contributes to a range of human diseases, most notably cardiovascular disease, inflammatory disorders and cancer.

Signaling to and from Integrins

Understanding the protein interaction networks that govern signaling to and from integrins is a major topic of research in the Calderwood lab. We, and others, have shown that direct binding of signaling, cytoskeletal and adaptor proteins to the short integrin cytoplasmic tails regulates integrin affinity for extracellular ligands, influences integrin clustering into adhesive structures and controls integrin recycling. Tail-binding proteins also link ligand-bound integrins to the actin cytoskeleton and activate signaling pathways. We seek to identify key proteins in integrin activation and signaling, structurally and biochemically characterize their interactions, and understand their functional significance in cell adhesion, migration and signaling.

For additional information please see our recent reviews: