Super-resolution microscopy reveals the nanoscale molecular architecture of 29 protein components of a eukaryotic contractile ring relative to the membrane.

A genetic approach documents that mitochondrial DNA moves from donor cells to recipient mtDNA-depleted cells in whole mitochondria and that this restores mitochondrial respiration and the capacity of the cells to form tumours.

Super-resolution microscopy reveals, at nanometric-scale, the highly organized protein structure of viroplasms, the viral factories used by rotavirus to replicate its genome and assemble new viral particles.

Although genetically and biochemically linked, the plant immune and growth receptors FLS2 and BRI1 form dispersed receptor clusters within the plasma membrane that are spatiotemporally separated.

Super-resolution microscopy and single particle tracking analysis of Piezo1 in red blood cells demonstrate its ability to sense membrane curvature, consistent with a force-through-membrane mechanism of channel mechanosensation in these cells.

Rhythmic centrifugal waves of auxin traveling through the tissue provides high definition positional information to cells that is not only spatial but also temporal.

Cryogenic super-resolution microscopy resolves the three-dimensional arrangement of individual fluorescent markers attached to protein complexes with Angstrom precision through their blinking behavior, polarization selection and a classification scheme.

Super-resolved architectural framework of subdistal appendages surprisingly reveals coupling between distal appendages and subdistal appendages.

The DCC-SMLM algorithm allows to determine protein oligomeric states in situ, using the information obtained from the colocalization of fluorescent markers, overcoming the need for extraction of proteins from cells or complicated experimental setups when using microscopy.