Browse our anti-Aurora A (AURKA) Antibodies

Fruit Fly (Drosophila melanogaster) Aurora Kinase A (AURKA) interaction partners

1. The data indicate that Aur-A depletion can elicit chromosome damage in Drosophila.

2. AURKA directly regulates mitochondrial functions and that AURKA over-expression promotes metabolic reprogramming by increasing mitochondrial interconnectivity.

3. WDR62 controls brain growth through lineage-specific interactions with master mitotic signaling kinase, aurora A kinase.

4. equatorial stimulation is mediated primarily by the delivery of factors to the cortex by noncentrosomal microtubules, as well as a midzone-derived phosphorylation gradient that is amplified by the concerted activities of mABK and a soluble pool of AAK.

5. Disrupting the spindle assembly checkpoint in the aurA mutant does not prevent neuroblast amplification, tumor formation or chromosome segregation.

6. Aurora A kinase activity contributes to phosphorylation of kinetochore substrates near poles and its inhibition results in chromosome misalignment and an increased incidence of erroneous kinetochore-MT attachments.

7. AurA and aPKC exert the spatiotemporal control of Lgl distribution to achieve unique cell polarity roles in distinct cell types.

8. Aurora A and B kinases directly phosphorylate Lgl to promote its mitotic relocalization.

9. Drosophila melanogaster aurora A phosphorylates the dynactin subunit p150(glued) on sites required for its association with the mitotic spindle.

10. One of the functions of Aurora A kinase is to direct centrosomal organization such that D-TACC complexed to the MSPS/XMAP215 microtubule-associated protein may be recruited, and thus modulate the behavior of astral microtubules.

11. Drosophila Aurora-A is required for centrosome maturation and actin-dependent asymmetric protein localization during mitosis.

12. Deletion mapping identifies a central domain of Aurora-A as essential for its centrosomal localization that is augmented by both the amino and the carboxyl terminal ends of the protein.

13. Results suggest that Aurora-A regulates centrosome assembly by controlling centrosomin's (CNN) ability to target and/or anchor gamma-tubulin to the centrosome and to organize microtubule-nucleating sites via interaction with CNN.

14. Aurora-A is essential for many crucial events during mitosis and phosphorylation of a series of substrates by Aurora-A at different stages of mitosis may promote diverse critical events in mitosis to maintain chromosome integrity in cells

15. identification of Bora, a conserved protein required for activation of Aurora-A at the onset of mitosis; model in which activation of Cdc2 initiates the release of Bora into the cytoplasm where it can bind and activate Aurora-A

16. Study shows that Aurora-A acts as a tumor suppressor by suppressing neuroblast self-renewal and promoting neuronal differentiation.

17. Study concludes that Aurora-A and Numb are novel inhibitors of neuroblast self-renewal and that spindle orientation regulates neuroblast self-renewal.

18. Study shows that a phosphorylation cascade triggered by the activation of Aurora-A is responsible for the asymmetric localization of Numb in mitosis.

19. Study identified a previously unrecognized evolutionarily conserved Pins domain (Pins(LINKER)) that requires Aurora-A phosphorylation to recruit Dlg and promote partial spindle orientation.

Zebrafish Aurora Kinase A (AURKA) interaction partners

1. Zebrafish Aurora-A is critically required for embryonic proliferation during development.

Human Aurora Kinase A (AURKA) interaction partners

1. Inhibition of AURKA led to strong cytotoxicity to gastric cancer cells with cytoplasmic p27 degradation and Bax cleavage, which were caused by activating the calpain pathway.

2. High AURORA-A expression is associated with radio-resistance of docetaxel-resistant Lung Adenocarcinoma.

3. Results found that over-expression and hyper-activation of AURORA A-PLK1-FOXM1 axis is only partly associated with the BCR-ABL1 TK activity and is enhanced by Imatinib (IM) resistance in chronic myeloid leukemia (CML). AURORA A-PLK1-FOXM1 over-expression induce IM resistance by activating multiple pathways implicated in proliferation and survival advantage of leukemic hematopoiesis.

4. AURKA polymorphisms are susceptible factors for oral cancer

5. Data suggest that this Plk1-PP6 interaction generates a feedback loop that coordinates and reinforces the activities of Plk1 and Aurora A during mitotic entry and is terminated by the degradation of Plk1 during mitotic exit. Thus, a mechanism for the previously puzzling observation of the Plk1-dependent regulation of Aurora A has been identified.

6. we took advantage of a chemical and chemical-genetic approach to specifically inhibit Aurora A kinase activity in late prometaphase. We observed that a loss of Aurora A activity directly affects SAC function, that Aurora A is essential for maintaining the checkpoint protein Mad2 on unattached kinetochores and that inhibition of Aurora A leads to loss of the SAC, even in the presence of nocodazole or Taxol.

7. Data indicate the roles and mechanisms of aurora kinase A (Aurora)-Polo-like kinase 1 (PLK1) signaling in the cell and centrosome cycles and in the DNA damage response{Review].

8. Study confirms that AURKA influences deregulation of Wnt and Ras-MAPK signaling genes in colorectal cancer (CRC)cell lines, and suggests mechanisms in CRC cell lines describing these interactions.

9. This study aimed at further elucidation of mechanisms governing cytotoxic activity of the anti-GD2 monoclonal antibody and the aurora A kinase specific inhibitor in the IMR-32 and CHP-134 human neuroblastoma cell lines, espe-cially in the context of the possible stimulation of autophagy

10. Study identified, for the first time, a functional crosstalk between protein kinase D2 (PKD2) and Aurora A kinase in cancer cells. The data demonstrate that PKD2 is catalytically active during the G2-M phases of the cell cycle, and inactivation or depletion of PKD2 causes delay in mitotic entry due to downregulation of Aurora A, an effect that can be rescued by overexpression of Aurora A.

11. we identified two modules with the AURKA gene and the DUSP1 gene as their cores. Interestingly, simultaneous activation of those genes was associated with the poorest prognosis in clinical samples.

12. AURKA acting as an effective biomarker for BC detection and prognosis, as well as therapeutic target

13. Molecular dynamics simulations and electron paramagnetic resonance experiments show that phosphorylation triggers a switch from an autoinhibited substate to an active substate, leading to catalytic activation.

14. temporal and spatial Aurora kinase-mediated regulation of SPICE1 is important for correct chromosome segregation.

15. knockdown of AURKA suppressed cell proliferation, migration and invasion, and also induced apoptosis and reactive oxygen species generation in Oral squamous cell carcinoma.

16. residual disease and acquired resistance in response to EGFR inhibitors requires Aurora kinase A (AURKA) activity.

17. Aurora A phosphorylation of YY1 during mitosis inactivates its DNA binding activity.

18. These results suggest that Aurora A activity is involved in the maintenance of Golgi architecture and the relationship between the Golgi apparatus and centrosome.

19. AURKA and HDAC2 genes were significantly overexpressed in all groups compared to the control. overexpression of AURKA genes was detected in the presence of metastasis and was up regulated during Gastric Cancer development.

20. Study indicated that AURKA, CDC20 and TPX2 are over-expressed in smoking related lung adenocarcinoma tissues and their higher mRNA expression levels have a worse prognosis.

Mouse (Murine) Aurora Kinase A (AURKA) interaction partners

1. in the absence of AURKC, AURKA localizes to chromosomes in a CPC-dependent manner. These data suggest that AURKC prevents AURKA from localizing to chromosomes by competing for CPC binding. This competition is important for adequate spindle length to support meiosis I. There is also a unique requirement for AURKB to negatively regulate AURKC to prevent aneuploidy.

2. AURKA is expressed in several cell types in the testis. Spermatogonia and spermatocytes express AURKA as expected based on the known role of this kinase in cell division. Surprisingly, we also found AURKA localized to spermatids and the flagellum of spermatozoa.

3. ex vivo cells derived from teratomas exhibited high self-renewal capacity that was linked to Aurora-A kinase activity and gave rise to lung metastasis when injected into the tail vein of immunocompromised mice.

4. Aurora A and Plk4 are rate-limiting factors contributing to microtubule growth as the acentriolar oocyte resumes meiosis.

5. The high sequence similarity among the AURK family members has made discerning the individual kinase functions in meiosis challenging. Technical limitations in specifically targeting AURKB or AURKC using small-molecule inhibitors and compensatory abilities in single-knockout animals add to this challenge...proper regulation of AURKA expression is crucial for spindle formation in meiosis

6. Aurora kinase inhibitor CCT137690 induces necrosis-like death in pancreatic ductal adenocarcinoma cells, via RIPK1, RIPK3, and MLKL signaling.

7. CIP2A acts as a scaffold for CEP192-mediated microtubule organizing center assembly by recruiting Plk1 and aurora A during meiotic maturation in mouse oocytes

8. AURKA stabilizes MYC to promote tp53-altered liver tumor cell survival.

9. Bcl2l10, Tpx2, and Aurka co-localized on the meiotic spindles, and Bcl2l10 was present in the same complex with Tpx2.

10. Suppression of neuroendocrine and NEPC development by ICT was associated with dose-dependent inhibitory effects on abnormally elevated IL-6/STAT3 and Aurora kinase A in vitro and in vivo

11. Our findings demonstrate that prolonged overexpression of Aurora-A can be a driver somatic genetic event in mammary adenocarcinomas associated with deregulated tumor-relevant pathways in the Aurora-A subset of human breast cancer

12. Data show that aurora-A kinase (AURKA) supports effective spindle formation in zygote.

13. observations revealed that the alteration of PKB-GSK-3beta axis, Plk-1, and Aurora kinase-A expressions in HSPC compartment due to DNA damage response was associated with the proliferative impairment and apoptosis during aplastic anemia.

14. Augmented expression of Aurora kinase-A and Polo-like kinase-1 at the lactogenic switch likely mediates the formation of binucleated cells.

15. Aurora A inhibition causes delocalized clustering of Lck at the immunological synapses and decreases its phosphorylation levels thus indicating Aurora A is required for maintaining Lck active during T-cell activation.

16. Ndel1 acts as a novel upstream regulator of the trichoplein-Aurora A pathway to inhibit primary cilia assembly.

17. The Aurora kinase A and c-Myc expression and histone H3 phosphorylation level were comparatively higher in the cranial tumor than the caudal.

18. aurora kinase A (AURKA) represents a new therapeutic target in primary myelofibrosis.

19. A novel function was identified for Aurora-A in controlling the polarization of macrophages and inflammation.

20. Wdr62 interacts with Aurora A to control mitotic progression, and loss of these interactions leads to mitotic delay and cell death of NPCs, which could be a potential cause of human microcephaly.

Cow (Bovine) Aurora Kinase A (AURKA) interaction partners

1. Aurora A was the most abundant form in oocytes, both at mRNA and protein levels, in bovine oocytes during meiotic maturation.

Pig (Porcine) Aurora Kinase A (AURKA) interaction partners

1. Aurora kinase A is unlikely to be involved in CPEB1 activating phosphorylation and cyclin B1 mRNA polyadenylation during meiotic maturation of porcine oocytes.

2. Aurora-A may be a multifunctional kinase that plays pivotal regulatory roles in microtubule assembly during porcine oocyte meiotic maturation, fertilization and early embryonic mitosis

3. Aurora A stimulates the protein synthesis and promotes the meiotic resumption.

Xenopus laevis Aurora Kinase A (AURKA) interaction partners

1. These results suggest a novel relationship between AurA and protein phosphatases during progression throughout the early embryonic cell cycle and shed new light on potential defects caused by AurA overexpression.

2. MCAK colocalized with NuMA and XMAP215 at the center of Ran asters where its activity is regulated by Aurora A-dependent phosphorylation of S196, which contributes to proper pole focusing

3. Plx1 promotes activation of Aurora A, most likely through TPX2.

4. Aurora-A kinase is required for astral microtubule polymerization and spindle microtubule flux during chromosome segregation.

5. Data show that Aurora A is a key regulator of microtubule assembly during M phase and therefore of bipolar spindle formation.

6. binding and elution properties of both the phosphopeptides and unphosphorylated peptides of His6-Aurora A

7. Results suggest that phosphorylation of maskin by Aurora-A prevents meiosis II proteins from being produced during meiosis I.

8. The N-terminal non-catalytic domain of Aurora-A can localize to the centrosome in Xenopus egg extracts, while GFP fusions of either the N-terminal or catalytic domains are targeted to the centrosome in Xenopus XL2 cells.

9. Here we identify G205 in Xenopus Aurora A as a key determinant of both intrinsic activity and regulation by TPX2

10. The catalytic domain alone of Aurora-A is sufficient to restore spindle bipolarity; additional N-terminal sequences function in mitotic timing.