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).

Conformational changes occur within extracellular domain of BCR upon antigen engagement, and these conformational changes are related with the strength of BCR activation and are distinct in IgM- and IgG-BCR.

The B cell receptors of naïve B cells need higher levels of mechanical force to be fully activated than those of memory B cells.

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

The immunoglobulin E (IgE) B cell receptor promotes plasma cell differentiation in the absence of cognate antigen and limits the competitive fitness of IgE⁺ B cells in germinal centers.

Protein kinase Cδ, a kinase downstream of B-cell antigen receptor, is found to be essential for class switching to and production of IgG in the T-cell-independent type 2 immune response and for regulation of gut-residing bacteria.

Arp2/3 complex-mediated actin polymerization shapes how B lymphocytes probe the surface of antigen-presenting cells, promotes coalescence of B cell receptor (BCR) microclusters, amplifies BCR signaling, and enhances B cell activation.

B-1 cell unresponsiveness to antigen-stimulation is overcome during infections when Toll-like receptor engagement removes negative regulators of B cell receptor signaling, thereby supporting B-1 cell differentiation to IgM-secreting plasmablasts.

The T-cell receptors of gamma delta (γδ) T cells can recognize and trigger responses to small molecules and are thereby versatile drivers of immunity.

The combination of molecular imaging, genetic and pharmacological approaches revealed that BCR signaling and PKCβ-dependent activation of focal adhesion kinase (FAK) is required for B cell mechanosensing.