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Protein aurora borealis (BORA) is a conserved cofactor essential for mitotic entry, acting primarily as a direct activator of Aurora kinase A (AURKA) during cell cycle progression. BORA is phosphorylated by CyclinA/B–Cdk1, then binds and activates AURKA, which in turn is necessary for the activation of polo-like kinase 1 (Plk1) by phosphorylating its T-loop[1]. This activation is mediated by specific motifs within BORA, notably two Tpx2-like motifs and a key phospho-Ser112 motif, which act together to stabilize and activate the kinase domain of AURKA. Rather than being a drug target itself, BORA serves as a critical regulatory hub at the G2/M transition, and aberrations in this regulatory axis can contribute to defective mitosis and have been implicated indirectly in cancer[1]. To date, there are no known therapeutics or approved drugs that directly target BORA, as it is not an enzyme, receptor, or transporter but functions as a scaffolding/cofactor protein essential for proper mitotic progression.
not applicable (BORA is a cofactor/activator, not a drug target)
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