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Disrupting the spindle assembly checkpoint in the aurA mutant does not prevent neuroblast amplification, tumor formation or chromosome segregation.
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.
AurA and aPKC exert the spatiotemporal control of Lgl distribution to achieve unique cell polarity roles in distinct cell types.
Aurora A and B kinases directly phosphorylate Lgl to promote its mitotic relocalization.
Drosophila melanogaster aurora A phosphorylates the dynactin (show DCTN1 Proteins) subunit p150(glued (show DCTN1 Proteins)) on sites required for its association with the mitotic spindle.
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.
Drosophila Aurora-A is required for centrosome maturation and actin-dependent asymmetric protein localization during mitosis.
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.
Results suggest that Aurora-A regulates centrosome assembly by controlling centrosomin's (CNN) ability to target and/or anchor gamma-tubulin (show TUBG1 Proteins) to the centrosome and to organize microtubule-nucleating sites via interaction with CNN.
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
Zebrafish Aurora-A is critically required for embryonic proliferation during development.
Authors conclude that AURKA may revive dormant tumor cells via FAK (show PTK2 Proteins)/PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) pathway activation, thereby promoting migration and invasion in laryngeal cancer.
our identification of the novel interaction between Aurora A and H-Ras (show HRAS Proteins) as a mechanism by which Aurora A can activate Ras-MAPK (show MAPK1 Proteins) signaling opens the way for studies into perturbation of the Aurora A/H-Ras (show HRAS Proteins) interaction and the effect on Ras-MAPK (show MAPK1 Proteins) signaling.
MiR (show MLXIP Proteins)-124-3p has significant impact on proliferation, migration and apoptosis of bladder cancer cells by targeting AURKA
Taken together, our data suggest that Aurora-A plays an important role in the suppression of autophagy by inhibiting the phosphorylation of Akt (show AKT1 Proteins), which in turn prevents autophagy-induced apoptosis in prostate cancer
Results show that overexpression of Aurora-A and PTGS2 (show PTGS2 Proteins) occurs in colon polyps and has a reverse correlation with miR (show MLXIP Proteins)-137 in both colon polyps and colorectal cancer tissue suggesting that AURKA and PTGS2 (show PTGS2 Proteins) expression is under the regulation of mir (show MLXIP Proteins)-137.
SIX3 is a novel negative transcriptional regulator and acts as a tumor suppressor that directly represses the transcription of AURKA and AURKB (show AURKB Proteins) in astrocytoma.
this report provides clear evidence that overexpression of the AURKA, SKA3 (show SKA3 Proteins), and DSN1 (show DSN1 Proteins) genes strongly correlates with the progression of colorectal adenomas to colorectal cancer
Although research biopsies were obtained on only a few patients, they did confirm pharmacodynamic effects of the drug. These effects though suggest inhibition of Aurora B (show AURKB Proteins) rather than Aurora A, which consistent with pre-clinical data that show dose-dependent effects on both
Aurora A kinase is hyperphosphorylated in early mitosis under oxidative stress, which may disturb the function of Aurora A in mitotic spindle formation.
Our findings suggested that AURKA (rs911160) and AURKB (show AURKB Proteins) (rs2289590) polymorphisms could affect GC risk. Further validation studies in larger and multi-ethnical populations are needed to elucidate their functional impact on the development of GC
Aurora A and Plk4 (show PLK4 Proteins) are rate-limiting factors contributing to microtubule growth as the acentriolar oocyte resumes meiosis.
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 (show AURKB Proteins) or AURKC (show AURKC Proteins) 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
Aurora kinase inhibitor CCT137690 induces necrosis-like death in pancreatic ductal adenocarcinoma cells, via RIPK1, RIPK3, and MLKL signaling.
CIP2A (show KIAA1524 Proteins) acts as a scaffold for CEP192-mediated microtubule organizing center assembly by recruiting Plk1 and aurora A during meiotic maturation in mouse oocytes
AURKA stabilizes MYC (show MYC Proteins) to promote tp53 (show TP53 Proteins)-altered liver tumor cell survival.
Bcl2l10 (show BCL2L10 Proteins), Tpx2 (show DAZL Proteins), and Aurka co-localized on the meiotic spindles, and Bcl2l10 (show BCL2L10 Proteins) was present in the same complex with Tpx2 (show DAZL Proteins).
Suppression of neuroendocrine and NEPC development by ICT was associated with dose-dependent inhibitory effects on abnormally elevated IL-6 (show IL6 Proteins)/STAT3 (show STAT3 Proteins) and Aurora kinase A in vitro and in vivo
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
Data show that aurora-A kinase (AURKA) supports effective spindle formation in zygote.
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.
Aurora A was the most abundant form in oocytes, both at mRNA and protein levels, in bovine oocytes during meiotic maturation.
Aurora kinase A is unlikely to be involved in CPEB1 (show CPEB1 Proteins) activating phosphorylation and cyclin B1 (show CCNB1 Proteins) mRNA polyadenylation during meiotic maturation of porcine oocytes.
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
Aurora A stimulates the protein synthesis and promotes the meiotic resumption.
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.
MCAK (show KIF2C Proteins) 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
Plx1 promotes activation of Aurora A, most likely through TPX2.
Aurora-A kinase is required for astral microtubule polymerization and spindle microtubule flux during chromosome segregation.
Data show that Aurora A is a key regulator of microtubule assembly during M phase and therefore of bipolar spindle formation.
binding and elution properties of both the phosphopeptides and unphosphorylated peptides of His6-Aurora A
Results suggest that phosphorylation of maskin (show TACC3 Proteins) by Aurora-A prevents meiosis II proteins from being produced during meiosis I.
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.
Here we identify G205 in Xenopus Aurora A as a key determinant of both intrinsic activity and regulation by TPX2
The catalytic domain alone of Aurora-A is sufficient to restore spindle bipolarity; additional N-terminal sequences function in mitotic timing.
The protein encoded by this gene is a cell cycle-regulated kinase that appears to be involved in microtubule formation and/or stabilization at the spindle pole during chromosome segregation. The encoded protein is found at the centrosome in interphase cells and at the spindle poles in mitosis. This gene may play a role in tumor development and progression. A processed pseudogene of this gene has been found on chromosome 1, and an unprocessed pseudogene has been found on chromosome 10. Multiple transcript variants encoding the same protein have been found for this gene.
A-type aurora kinase
, aurora A
, aurora A kinase
, aurora kinase
, Aurora A
, hypothetical protein
, aurora kinase A
, serine/threonine-protein kinase 6
, serine/threonine protein kinase 6
, aurora A kinase protein
, serine/threonine-protein kinase 6-like
, Aurora-A kinase
, IPL1-related kinase
, aurora 2
, aurora-related kinase 1
, aurora/IPL1-like kinase
, aurora/IPL1-related kinase 1
, breast tumor-amplified kinase
, breast-tumor-amplified kinase
, protein phosphatase 1, regulatory subunit 47
, serine/threonine kinase 6
, serine/threonine protein kinase 15
, serine/threonine-protein kinase 15
, serine/threonine-protein kinase aurora-A
, aurora family kinase 1
, ipl1- and aurora-related kinase 1
, serine/threonine-protein kinase Ayk1
, Serine/threonine-protein kinase 6
, aurora kinase A-A
, serine/threonine-protein kinase 6-A
, serine/threonine-protein kinase Eg2
, serine/threonine-protein kinase Eg2-A