NEK7 Protein, Human (Inactive, sf9, His-GST)

NEK7 protein, a pivotal kinase, plays a crucial role in mitotic cell cycle progression by contributing to the microtubule nucleation activity of the centrosome, ensuring robust mitotic spindle formation, and facilitating cytokinesis. Its diverse functions include the phosphorylation of EML4 at 'Ser-146,' promoting dissociation from microtubules during mitosis and thereby facilitating efficient chromosome congression. NEK7 extends its impact beyond mitotic events by phosphorylating RPS6KB1 and serving as an essential activator of the NLRP3 inflammasome assembly. Independently of its kinase activity, NEK7 unlocks NLRP3 within the microtubule organizing center, promoting the formation of the NLRP3:PYCARD complex and activation of CASP1. Notably, NEK7 acts as a cellular switch, ensuring mutual exclusivity between the inflammasome response and cell division; its interaction with NEK9 prevents interaction with NLRP3 and inflammasome activation during mitosis. These multifaceted functions position NEK7 as a key orchestrator in both mitotic progression and the inflammasome response, highlighting its regulatory significance in diverse cellular processes.