Integrins are transmembrane adhesion receptors that link the extracellular matrix to the cytoskeleton. We study how integrins transmit conformational and mechanical signals across the membrane, connecting ligand binding to cytoskeletal dynamics and force generation. Using cryo-EM, FRET reporters with non-canonical amino acids, and single-molecule tools such as magnetic and laser tweezers, we dissect how conformational transitions between bent-closed, extended-closed, and extended-open states drive activation. These studies reveal how hybrid-domain swing-out and βI-domain rearrangements produce long-range allosteric effects that tune adhesion. At the cellular level, we investigate how integrins such as α4β1, α4β7, LFA-1, Mac-1, and αIIbβ3 mediate rolling and firm adhesion in leukocyte trafficking and platelet aggregation under flow. Building on decades of integrin structural biology, we now engineer integrin agonists that stabilize specific conformations to precisely control cell behavior, differentiation, and tissue organization.

We are integrating our understanding of integrin signaling with organoid and stem cell biology to engineer defined, animal-free extracellular environments that support tissue growth and maturation. By coupling integrin agonists with synthetic hydrogels, we aim to create reproducible, scalable systems for organoid culture and regenerative medicine. These efforts connect fundamental receptor biology to practical platforms for disease modeling, tissue engineering, and drug development.