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Hardwick, K.

Publications and source records attributed to Hardwick, K..

2 recordsLinked to original sources

Cryptococcus neoformans employs both PP1 and PP2A phosphatases to silence the spindle checkpoint

The spindle checkpoint preserves genomic integrity by delaying anaphase onset until all kinetochores achieve bi-polar microtubule attachment. While checkpoint activation is well-characterised across eukaryotes, the mechanisms governing its silencing remain less defined and are more variable in different systems. In this study, we reveal that the fungal pathogen Cryptococcus neoformans employs a dual phosphatase-mediated mechanism to silence the spindle checkpoint. We show that PP1 is recruited to kinetochores by Spc105KNL1, via conserved SILK and RVSF motifs, while PP2A-B56 is recruited to kinetochores through direct Bub1 binding via an LxxIxE motif. Disruption of either recruitment pathway leads to prolonged checkpoint signalling and mitotic defects, underscoring the critical roles of these phosphatases in checkpoint silencing and mitotic exit. These findings further establish C. neoformans as a powerful model for studying mitotic regulation in the basidiomycete lineage and identify phosphatase recruitment interfaces as potential targets for antifungal intervention.

cell biology↗

mps1 and mad mutations reduce Cryptococcus neoformans titan cell viability

Cryptococcus neoformans is an opportunistic, human fungal pathogen which undergoes fascinating switches in cell cycle control and ploidy when it encounters stressful environments such as the human lung. Here we carry out a mechanistic analysis of the spindle assembly checkpoint (SAC) which regulates the metaphase to anaphase transition, focusing on Mps1 kinase and the downstream checkpoint components Mad1 and Mad2. We demonstrate that Cryptococcus mad1{Delta} or mad2{Delta} strains are unable to respond to microtubule perturbations, continuing to re-bud and divide, and die rapidly as a consequence. Fluorescent tagging of Chromosome 3, using a lacO array and mNeonGreen-lacI fusion protein, demonstrates that mad mutants are unable to maintain sister-chromatid cohesion in the absence of microtubule polymers. Thus, the classic checkpoint functions of the SAC are conserved in Cryptococcus. In interphase, GFP-Mad1 is enriched at the nuclear periphery, and it is recruited to unattached kinetochores in mitosis. Purification of GFP-Mad1 followed by mass spectrometric analysis of associated proteins show that that it forms a complex with Mad2 and that it interacts with other checkpoint signalling components (Bub1) and effectors (Cdc20 and APC/C sub-units) in mitosis. We also demonstrate that overexpression of Mps1 kinase is sufficient to arrest Cryptococcus cells in mitosis, and show that this arrest is dependent on both Mad1 and Mad2. We find that a C-terminal fragment of Mad1 is an effective in vitro substrate for Mps1 kinase and map several Mad1 phosphorylation sites. Some sites are highly conserved within the C-terminal Mad1 structure and we demonstrate that mutation of threonine 667 (T667A) leads to loss of checkpoint signalling and abrogation of the GAL-MPS1 arrest. Thus Mps1-dependent phosphorylation of C-terminal Mad1 residues is a critical step in Cryptococcus spindle checkpoint signalling. Finally, we analyse the phenotype of mad and mps1 mutants during titan cell generation: quantitating viability of titan cells and their daughters generated during the ensuing reductive division. The mad1{Delta}, mad2{Delta} and mps{Delta} mutants show significantly reduced viability: many titans are dead and others produce slow growing colonies. We propose that these Cryptococcus neoformans checkpoint proteins have important roles in ensuring high fidelity chromosome segregation during stressful conditions, such that those heightened during its polyploid infection cycle.

cell biology↗