| 1 |
IPD2610 |
Divergent Plasmodium Aurora related kinases ARK1 and ARK2 coordinate spindle biogenesis and karyokinesis by regulating key centromere-kinetochore proteins |
Dr. T S Keshava Prasad |
Human malaria parasite Plasmodium falciparum is a unicellular eukaryote that proliferates within human and mosquito hosts via highly specialized cell division processes that are markedly different from those of conventional eukaryotic model organisms. Aurora kinases are central regulators of eukaryotic cell division. Although Plasmodium species encode three divergent Aurora-related kinases...
Human malaria parasite Plasmodium falciparum is a unicellular eukaryote that proliferates within human and mosquito hosts via highly specialized cell division processes that are markedly different from those of conventional eukaryotic model organisms. Aurora kinases are central regulators of eukaryotic cell division. Although Plasmodium species encode three divergent Aurora-related kinases (ARK1–3) that are essential for parasite survival. In this study, we show that conditional knockout of PfARK2 disrupts spindle formation, leading to defects in karyokinesis and subsequent failure of cytokinesis. Recently, we reported similar role for PfARK1; however, the underlying mechanisms remained unclear. Phosphoproteomic analyses reveal that PfARK1 and PfARK2 target distinct sets of substrates, several of which are key kinetochore proteins. Strikingly, PfARK2 regulates the phosphorylation-dependent localization of PfCENH3, a centromere-specific histone H3 variant essential for spindle assembly and nuclear division. NUF2, an outer kinetochore component, is differentially regulated by both kinases at distinct sites. The regulation of these proteins by PfARK1/2 is critical for proper kinetochore assembly and spindle formation. Furthermore, we have identified small-molecule inhibitors targeting these Aurora kinases that effectively block asexual stage proliferation of P. falciparum by disrupting PfARK1/2-dependent processes. These findings provide novel insights into parasite division and highlight a promising avenue for the development of novel antimalarial therapies.
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NITTE, Deemed to be University, Mangaluru, Karnataka, India |
Bottom-up |
2027-06-04 |
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| 2 |
IPD9272 |
From Omics to Function: NCU05627 Emerges as a Pivotal Sugar Transporter for Cellulase Secretion in Neurospora crassa |
Dr. Nidhi Adlakha |
This study investigates the role of sugar transporters in cellulase secretion and polysaccharide utilization in Neurospora crassa using an LC–MS/MS-based proteomics approach. Comparative proteomic profiling identified 2480 proteins shared between the experimental conditions, including several upregulated sugar transporters and carbohydrate-active enzymes (CAZymes) associated with biomass degradation. Functional annotation through Gene...
This study investigates the role of sugar transporters in cellulase secretion and polysaccharide utilization in Neurospora crassa using an LC–MS/MS-based proteomics approach. Comparative proteomic profiling identified 2480 proteins shared between the experimental conditions, including several upregulated sugar transporters and carbohydrate-active enzymes (CAZymes) associated with biomass degradation. Functional annotation through Gene Ontology analysis revealed enrichment of proteins involved in catalytic activity and metabolic processes. Among the identified sugar transporters, the putative xylose transporter NCU05627 was selected for further characterization due to its previously uncharacterized role in cellulase induction. Phylogenetic analysis grouped NCU05627 within the hexose transporter-enriched clade, suggesting a conserved role in sugar uptake. Functional studies demonstrated that deletion of NCU05627 reduced the secretion of plant cell wall-degrading enzymes. This dataset provides comprehensive insight into the sugar transportome of N. crassa and identifies transporter proteins potentially involved in cellulose degradation and fungal biomass conversion.
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DBT-Regional Centre for Biotechnology, Haryana, Faridabad, India |
Bottom-up |
2027-12-31 |
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