ArticleJournal of cell science2015
A non-mitotic role for Aurora kinase A as a direct activator of cell migration upon interaction with PLD, FAK and Src.
Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
25 citing papers in PubMed, 44 citations in OpenAlex.
- NN-01-195, a Novel Conjugate of HSP90 and AURKA Inhibitors, Effectively Targets Solid Tumors.Molecular cancer therapeutics · 2026Article
- The significant others of aurora kinase a in cancer: combination is the key.Biomarker research · 2024Review
- PLK1 inhibition dampens NLRP3 inflammasome-elicited response in inflammatory disease models.The Journal of clinical investigation · 2023Article
- Aurora Kinase A Regulation by Cysteine Oxidative Modification.Antioxidants (Basel, Switzerland) · 2023Review
- The Recurrent-Specific Regulation Network of Prognostic Stemness-Related Signatures in Low-Grade Glioma.Disease markers · 2023Article
- ISL1 promoted tumorigenesis and EMT via Aurora kinase A-induced activation of PI3K/AKT signaling pathway in neuroblastoma.Cell death & disease · 2021Article
- Adhesion-growth factor crosstalk regulates AURKB activation and ERK signalling in re-adherent fibroblasts.Journal of biosciences · 2021Article
- Structure and regulation of human phospholipase D.Advances in biological regulation · 2021Review
- Article
- Insights into the non-mitotic functions of Aurora kinase A: more than just cell division.Cellular and molecular life sciences : CMLS · 2020Review
- Random-forest algorithm based biomarkers in predicting prognosis in the patients with hepatocellular carcinoma.Cancer cell international · 2020Article
- Phospholipase D2 in prostate cancer: protein expression changes with Gleason score.British journal of cancer · 2019Article
- RACK1 affects the progress of G2/M by regulating Aurora-A.Cell cycle (Georgetown, Tex.) · 2019Article
- hnRNPK S379 phosphorylation participates in migration regulation of triple negative MDA-MB-231 cells.Scientific reports · 2019Article
- Molecularly annotation of mouse avatar models derived from patients with colorectal cancer liver metastasis.Theranostics · 2019Article
- Targeting AURKA-CDC25C axis to induce synthetic lethality in ARID1A-deficient colorectal cancer cells.Nature communications · 2018Article
- Oxidized LDL phagocytosis during foam cell formation in atherosclerotic plaques relies on a PLD2-CD36 functional interdependence.Journal of leukocyte biology · 2018Article
- The functional diversity of Aurora kinases: a comprehensive review.Cell division · 2018Review
- UBE2C induces EMT through Wnt/β‑catenin and PI3K/Akt signaling pathways by regulating phosphorylation levels of Aurora-A.International journal of oncology · 2017Article
- GAK is phosphorylated by c-Src and translocated from the centrosome to chromatin at the end of telophase.Cell cycle (Georgetown, Tex.) · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Timely activation of Aurora kinase A (AURA, also known as AURKA) is vital for centrosome formation and the progression of mitosis. Nonetheless, it is still unclear if and when other cellular functions are activated by AURA. We report here that Src phosphorylates and activates AURA at T288, and AURA also activates focal adhesion kinase (FAK, also known as PTK2), leading to initiation of cell movement. An additional and new way by which AURA is regulated, is by phospholipase D2 (PLD2), which causes AURA activation. In addition, AURA phosphorylates PLD, so both proteins engage in a positive reinforcement loop. AURA and PLD2 form a protein–protein complex and colocalize to cytoplasmic regions in cells. The reason why PLD activates AURA is because of the production of phosphatidic acid by the lipase, which binds directly to AURA, with the region E171–E211 projected to be a phosphatidic-acid-binding pocket. Furthermore, this direct interaction with phosphatidic acid enhances tubulin polymerization and cooperates synergistically with AURA, FAK and Src in yielding a fully effectual cellular migration. Thus, Src and FAK, and PLD and phosphatidic acid are new upstream regulators of AURA that mediate its role in the non-mitotic cellular function of cell migration.
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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.