NEK2

NEK2 (NIMA-related kinase 2) is a serine/threonine kinase that localizes predominantly to the centrosome and functions as a key regulator of centrosome separation, bipolar spindle assembly, chromosome segregation, and mitotic progression^[1][2][3]. NEK2 expression increases during S and G2 phases of the cell cycle, supporting its role in coordinating accurate cell division and maintenance of genomic stability^[2][3]. Mechanistically, NEK2 phosphorylates proteins involved in centrosome disjunction and chromosome segregation, and dysregulated NEK2 activity promotes premature centrosome splitting, chromosomal instability, aneuploidy, and aberrant mitotic progression^[1][4][5]. In addition to its canonical centrosomal functions, NEK2 can localize to the nucleus, interact with splicing factors, and regulate alternative splicing programs linked to cell survival and apoptosis^[4]. In disease contexts, NEK2 is frequently overexpressed in multiple malignancies, where elevated expression is associated with tumor progression, drug resistance, chromosomal instability, and poor clinical prognosis^[5][6]. Compared with other members of the NIMA-related kinase family, NEK2 is distinguished by its prominent role in centrosome dynamics and mitotic regulation, and alternative splicing generates isoforms with distinct C-terminal regions that may differ in subcellular localization and regulatory properties^[2][3]. For experimental applications, NEK2 has emerged as a therapeutic target, and small-molecule inhibitors have demonstrated the ability to suppress NEK2 kinase activity in cellular and preclinical cancer models, supporting their utility for investigating mitotic regulation and cancer biology^[5][7].