ArticleMolecular biology of the cell2019
A rapid computational approach identifies SPICE1 as an Aurora kinase substrate.
Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- CDK1 and CEP97 cooperatively control centriole length to orchestrate ciliogenesis and developmental patterning.Genes & development · 2026Article
- Molecular basis for the activation of Aurora A and Plk1 kinases during mitotic entry.The EMBO journal · 2026Article
- SPICE1 promotes osteosarcoma growth by enhancing the deubiquitination of FASN mediated by USP10.Journal of translational medicine · 2025Article
- Aurora A kinase inhibition compromises its antitumor efficacy by elevating PD-L1 expression.The Journal of clinical investigation · 2023Article
- Aurora Kinase A proximity map reveals centriolar satellites as regulators of its ciliary function.EMBO reports · 2021Article
- Mitotic HOOK3 phosphorylation by ERK1c drives microtubule-dependent Golgi destabilization and fragmentation.iScience · 2021Article
- Article
- Phospho-regulation of mitotic spindle assembly.Cytoskeleton (Hoboken, N.J.) · 2020Review
- Dissecting the mechanisms of cell division.The Journal of biological chemistry · 2019Review
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Aurora kinases play a major role in mitosis by regulating diverse substrates. Defining their critical downstream targets is important in understanding Aurora kinase function. Here we have developed an unbiased computational approach to identify new Aurora kinase substrates based on phosphorylation site clustering, protein localization, protein structure, and species conservation. We validate the microtubule-associated proteins Clasp2, Elys, tubulin tyrosine ligase-like polyglutamylase residues 330-624 and spindle and centriole associated protein 1, residues 549-855 (SPICE1), as Aurora A and B kinases substrates in vitro. We also demonstrate that SPICE1 localization is regulated by Aurora kinases during mitosis. In the absence of Aurora kinase activity, SPICE1 remains at centrioles but does not target to the spindle. Similarly, a nonphosphorylatable SPICE1 mutant no longer localizes to the spindle. Finally, we show that misregulating SPICE1 phosphorylation results in abnormal centriole number, spindle multipolarity, and chromosome alignment defects. Overall, our work indicates that temporal and spatial Aurora kinase-mediated regulation of SPICE1 is important for correct chromosome segregation. In addition, our work provides a database-search tool that enables rapid identification of Aurora kinase substrates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.