Compositional changes alter actin binding by phase separated T cell signaling clusters, enabling cluster movement by distinct actin networks.

Inhibition of the catalytic activity of the Zap70 kinase reveals that discrete TCR-regulated events control the remodelling of the actin cytoskeleton when the cytotoxic T cell interacts with its target.

Studying the earliest events in B cell activation reveals that the B cell antigen receptor is opened and activated via the phosphorylation and binding by the spleen tyrosine kinase (Syk).

T cell receptor signaling is regulated by newly polymerized F-actin foci at the immunological synapse.

A membrane-associated, supramolecular protein complex with dynamically changing components, the central supramolecular activation cluster, regulates the generation of the T cell effector cytokine IL-2 depending on its composition.

A light-controllable ligand is used to probe where in the signaling cascade T cells discriminate self from non-self.

Direct control of ligand binding half-life with light shows that lifetime strongly affects T cell signaling.

A designer peptide inhibits the T cell receptor through allosteric binding to the transmembrane region.

Single-molecule localization imaging shows that the Nipah virus fusion protein forms nanoscale clusters on cell and viral membranes that favor membrane fusion activation.

Sorting nexin 9, a membrane curvature inducing protein, creates a distinct environment within clusters of the co-receptor CD28 and thereby allows T cell activation to proceed to a successful outcome.