ArticleEMBO reports2026
Bora bridges Aurora-A activation and substrate recognition of PLK1.
Article in EMBO reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Bora, CEP192 and Cenexin regulate distinct Plk1-dependent cell and centrosome cycle transitions.Nature communications · 2026Article
- Molecular requirements for PLK1 activation by T-loop phosphorylation.The EMBO journal · 2026Article
- Mitotic entry: Bora takes Polo to Aurora, and gives them a hug.The EMBO journal · 2026Article
- Molecular basis for the activation of Aurora A and Plk1 kinases during mitotic entry.The EMBO journal · 2026Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The activation of PLK1 in late G2 is critical for mitotic entry, requiring its phosphorylation by Aurora-A, facilitated by the intrinsically disordered protein Bora. The structural basis of this mechanism has remained unresolved. Here, we present models of the Aurora-A/Bora complex and the Aurora-A/Bora/PLK1 complex, validated with site-specific mutagenesis, biochemical assays and NMR spectroscopy. Bora wraps around the N-lobe of Aurora-A, occupying the pockets used by its other activators. A CDK1 phosphorylation site on Bora (Ser112) mimics the structural role of Aurora-A activation loop phosphorylation within a TPX2-like binding motif. In the ternary complex, Bora bridges the two kinases, orienting the activation loop of PLK1 towards the active site of Aurora-A. Bora residues 56-66 form a critical interface with a conserved pocket on the PLK1 C-helix that is analogous to the TPX2-binding Y-pocket of Aurora-A. Aurora-A phosphorylation of Bora Ser59 creates an additional interaction that increases the efficiency of PLK1 phosphorylation. These findings deepen our understanding of Aurora-A regulation by its disordered binding partners and establish a mechanistic framework for Bora-dependent activation of PLK1.
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Registered trials
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