We are excited about this study as multiple studies had suggested that such an outer kinetochore receptor for Aurora B must exist. We feel it’s an important step towards understanding how Ipl1/Aurora B achieves tension-dependent substrate phosphorylation at the outer kinetochore.

Alex shows that the mutant is very sensitive to a reduction in Ipl1 activity. However, it can be rescue it by recruitment of active Ipl1 to KMN in vivo. Biochemically Ipl1-Sli15 binds reconstituted KMN via Spc105-Kre28 in vitro, the binding is counteracted by Ipl1 phosphorylation

Alex’ work describes a new mutant in the outer kinetochore KMN subunit Kre28/Zwint. This allele is intriguing because it resembles mutants in the tension-dependent error correction pathway such as ipl1, sli15 or sgo1.

Congratulations to our PhD student Sharvari for submitting her thesis. #Bub1licious

On our way to #cellbio2023. Visit us at our posters P2643, P2645 and P2670 on Tuesday 12:15-15:15. We are happy to discuss our research with you.

Welcome to our new PhD student @Sonja_Hbrkrn, who will work on the fate of inner kinetochore subunits.

The surface on Ndc80c that binds Mps1 also serves as interface for the Ipl1 regulated engagement of Dam1 at bi-oriented kinetochores. Dam1 competes with Mps1 in vitro and Dam1 mutants that mimic Ipl1 phosphorylation cannot displace Mps1 efficiently.

One conserved feature of the interaction is that it is negatively regulated byMps1 autophosphorylation. We mapped autophosphorylation sites in Mps1 and showed that phosphorylation contributes but is not sufficient for the release of Mps1 before anaphase.

In the manuscript, define a binding interface of Mps1 on Ndc80c, located on the backside of the CH-domains. Point mutations derived from the structure impair the Mps1:Ndc80c interaction in vitro and generate in Mps1 separation-of-function alleles in vivo.

Lab retreat at the zoo :) #retreat #kinetochoreandmore #fun