For initiation of cell-wall insertion, the cross-linking enzyme PBP2 stably binds to a component of the cell envelope that is different from MreB filaments.

Cryo-electron tomography of close-to-native rod outer segments resolves connectors between disks and a scaffold at the disk rim enforcing the high membrane curvature of the unique long-range organization in these rhodopsin-rich light-sensitive subcellular organelles.

Serine and threonine phosphorylation sites work in concert to provide rapid and reproducible desensitization of the G-protein coupled receptor rhodopsin.

Each cone terminal is electrically coupled to around 50 nearby rods, forming a switchable circuit, known as the secondary rod pathway, in which all gap junction channels participate.

MreB filaments bind, orient, and move along the direction of greatest membrane curvature, thus orienting the insertion of new glycan strands around the cell circumference in a manner that may help establish and maintain rod shape.

The 'spinning lasso' geometry of Euglena's beating flagellum is revealed, and a model based on the antagonistic forces exchanged by axoneme and paraflagellar rod is proposed to explain its emergence.

Class-A penicillin-binding proteins are dispensable for rod-like cell-shape but essential for mechanical integrity by sensing and repairing cell-wall defects locally, as investigated in the model system Escherichia coli.

The pentameric condensin II complex is equipped with a multilayered, self-regulatory mechanism that supports mitotic chromosome assembly.

A structural and biochemical study of human SYCP3 provides the first molecular model for the three-dimensional organisation that is imposed upon chromosomal DNA during meiosis and is essential for genetic exchange and fertility.

Dominant mutations in Arl3, linked to inherited retinal dystrophy, disrupt the active Arl3-GTP ciliary gradient and cause a defect in rod photoreceptor nuclear migration that can be rescued by elevating ciliary Arl3 activity or reducing aberrant non-ciliary Arl3 activity.