A phase transition of TIR-1/SARM1 induced by either pathogen or non-pathogen stress potentiates its intrinsic NADase activity, which activates the p38 PMK-1 signaling cascade to induce protective immune defenses in Caenorhabditis elegans intestinal epithelial cells.

TIR-1 regulates both repair and destruction on either side of an injury axon.

Genetic analyses reveal that the TIR1/AFB auxin receptors have broadly overlapping functions throughout plant development, but that the AFB1 receptor has a specialized role in a rapid auxin response.

Biophysical and structural studies reveal how low piconewton forces across actin enhance binding by the critical cell-cell adhesion protein α-catenin versus its force insensitive homolog vinculin.

The strength of Toll-like receptor signalling depends on the number and size of MyDDosomes formed as well as on how quickly these structures assemble.

The nuclear pathway for auxin perception is responsible for the rapid auxin-induced cell wall acidification and growth of aerial organs of plants.

Experiments in mice have shown than an enzyme that repairs broken DNA inside the nucleus also has a central role in the innate immune system because it is able to detect foreign DNA outside the nucleus.

TIRF microscopy in living pancreatic beta cells lacking one or two of Rab27 effectors and the exocyst components reveals how each molecule functions in sequence or in parallel in multiple redundant paths and rate-limiting processes in granule exocytosis.

The kinetics of actin polymerization are strongly influenced by the binding of proteins to the lateral filament surface.

A single-molecule biophysical approach reveals that the C-terminal domain of ParB blocks ParB network formation by heterodimerization with the full-length protein, which remains bound to the DNA.