Ligand binding, force and chemistry combine to control the function of a cell surface receptor.

Integrons deploy a variety of adaptive strategies including excision, shuffling, and duplication of cassettes that foster rapid bacterial adaptation and resistance evolution while protecting the genomic integrity of the host.

Diverse biophysical properties of β1 and β3 integrin transmembrane and cytoplasmic domains result in distinct mechanisms of integrin activation and function.

Kindlin-2 co-operates with talin to activate fibronectin-binding integrins on fibroblasts and subsequently induces cell spreading by recruiting paxillin to small, peripheral nascent adhesions.

Biochemical and cell biological data suggest a model of nascent integrin adhesion complex formation based on synergistic phase separation of pathways surrounding the focal adhesion kinase (FAK) and the adaptor protein p130Cas.

Caveolae regulate integrin mechanosensing by establishing a force threshold for activation and recycling.

Integrin and actin associated proteins are resolved into four layers within myofibril attachments, an architecture requiring balanced positive and negative regulation of integrin adhesion with integrated mechanotransduction and actin pathways.

Characterization of Tnc as a selective integrin ligand at the Drosophila NMJ allows for unprecedented insights into our understanding of extracellular matrix/integrin interactions at synaptic locations and reveals novel, distinct presynaptic and postsynaptic integrin functions.

In response to disruption of barrier functions mediated by septate junctions, Drosophila epithelial cells restrict endosomal degradation of transmembrane cell adhesion proteins to promote their recycling in order to maintain tissue integrity.

B-cell integrin co-stimulation promotes the formation of an actomyosin network that drives integrin-dependent immune synapse formation and B-cell activation.