The spindle assembly protein Bub3 recruits the checkpoint kinase Bub1 to kinetochores by binding to phosphorylated MELT repeats in the kinetochore subunit Knl1.
Nonlinear receptive field subunits in retinal ganglion cells are isolated and characterized by clustering spike-triggered stimuli, and validated on population responses to naturalistic and novel closed loop stimuli.
Direct live-cell imaging of human cells, combined with RNA-seq, qPCR and in vitro reconstitution essays, reveal that mitotic progression, arrest, exit or death is independent of de novo transcription.
Chromosome segregation in male spermatocytes exhibits anaphase A without shortening of autosome-associated microtubules and partitioning of an unpaired X chromosome that is initiated by an imbalance of attached kinetochore microtubules.
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.
The spindle checkpoint kinase Mps1 sequentially phosphorylates multiple substrates to amplify checkpoint signals, making the checkpoint highly dependent on Mps1 function and directly responsive to kinetochore-microtubule attachment.
Human chromosome-microtubule attachments are stabilised by Astrin-mediated dynamic delivery of PP1 phosphatase to the attachment site, which ensures the normal segregation of chromosomes.
The centromeric protein CENP-T assembles the microtubule-binding interface of kinetochores through direct recruitment of two Ndc80 complexes and indirect recruitment of a third one through the Mis12 complex.
