The spindle assembly protein Bub3 recruits the checkpoint kinase Bub1 to kinetochores by binding to phosphorylated MELT repeats in the kinetochore subunit Knl1.

Cell biological and genetic analyses reveal how budding yeast cells optimize Spindle Assembly checkpoint signaling to maximize chromosome segregation accuracy and minimize unnecessary delays in anaphase onset.

A synthetic, prospective article considers how the fields of sensory ecology and collective behaviour can combine when considering animal collective movements and interactions, and how these fields can inspire each other to advance understanding of animal behaviour, adaptation and evolution.

Environmental DNA from highly standardized leaf sample time series suggests no localized species losses, but biotic turnover and homogenization, as main drivers of forest insect decline.

Fungal hyphae constantly undergo signal oscillations, comparable to a cell 'monologue' until they meet another hypha with which they then coordinate signal oscillations and transit into a cell-to-cell dialogue.

At optimal concentrations, the ciliary inhibitor Cp110 promotes ciliogenesis by localization to previously uncharacterized sites at the basal body, where it recruits ciliary adhesion complexes that mediate basal body interaction with F-actin networks.

Tools and methodologies to create and diversify recombinant antibodies and antibody fragments provide researchers with the ability to generate low-cost, high-yield immunological reagents.

CMG helicase translocates with force while encircling duplex DNA, enabling two opposing CMG complexes at an origin to melt the duplex and switch to encircling separate single strands.

A structural study reveals how the simian virus 40 Large-T hexamer helicase interacts with its origin DNA and partially melts the origin double-stranded DNA within the hexamer channel.

The mechanism behind the recruitment of the spindle assembly checkpoint protein BubR1 to the kinetochore illustrates how gene duplication and sub-functionalization can influence the functional complexity of a protein network.