X-ray crystallography reveals that the Dna2 nuclease-helicase contains a long tunnel through which single-stranded DNA threads, and an allosteric mechanism for displacing the DNA-binding protein Rpa that restricts cleavage to the proper polarity.

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.

Selective involvement of Arp2/3 complex subunit isoforms ARPC5 or ARPC5L governs the distinct actin polymerization events in the nucleus or cytoplasm of CD4 T cells that are triggerd by T cell activation or DNA replication stress.

Pigmentation that confers protective function of RPE is not underlaid by a specific gene expression profile, reviled by microscopic imaging together with single-cell RNA sequencing.

Plexin controls the spatial distribution of synapses by locally inhibiting Rap2 small GTPase activity along the axon, and a Rap2 effector, TNIK, which also plays a key role in inhibiting synapse number.

Single-molecule TIRF microscopy, biochemical assays and mathematical modeling demonstrate how actin-branch nucleation by the Arp2/3 complex is coordinately regulated by two biochemically distinct activators.

Kidney organoids are a high-fidelity system for investigating basement membrane regulation in development and disease.

The essential mycobacterial transcription factor RbpA interacts with promoter DNA and cooperates with another essential transcription factor, CarD, to stimulate the formation of an intermediate leading to the open promoter complex.

Ensemble cryo-EM visualizes how structural rearrangements poise the newly made protein and release factor RF2 to dissociate in preparation for ribosome recycling.

Cryo-EM structures reveal the structural dynamics of ArfA*RF2-mediated rescue of stalled ribosomes.