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Aurora kinase B

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AURKB
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAURKB, AIK2, AIM-1, AIM1, ARK2, AurB, IPL1, PPP1R48, STK12, STK5, aurkb-sv1, aurkb-sv2, aurora kinase B, STK-1, ARK-2
External IDsOMIM: 604970; MGI: 107168; HomoloGene: 55807; GeneCards: AURKB; OMA:AURKB - orthologs
Orthologs
SpeciesHumanMouse
Entrez

9212

20877

Ensembl

ENSG00000178999

ENSMUSG00000020897

UniProt

Q96GD4

O70126

RefSeq (mRNA)

NM_011496

RefSeq (protein)

NP_035626

Location (UCSC)Chr 17: 8.2 – 8.21 MbChr 11: 68.94 – 68.94 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Aurora kinase B is a protein that functions in the attachment of the mitotic spindle to the centromere and in cytokinesis.

Function

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Chromosomal segregation during mitosis as well as meiosis is regulated by kinases and phosphatases. The Aurora kinases associate with microtubules during chromosome movement and segregation. Aurora kinase B localizes to microtubules near kinetochores, specifically to the specialized microtubules called K-fibers, and Aurora kinase A (MIM 603072) localizes to centrosomes (Lampson et al., 2004).[supplied by OMIM][5]

In cancerous cells, over-expression of these enzymes causes unequal distribution of genetic information, creating aneuploid cells, a hallmark of cancer.

Discovery

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In 1998, Aurora kinase B was identified in humans by a polymerase chain reaction screen for kinases that are overexpressed in cancers.[6] In the same year, rat Aurora kinase B was identified in a screen designed to find kinases that altered S. cerevisiae proliferation when overexpressed.[7]

Expression and subcellular localization

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Aurora kinase B (in green) localizes in a cell cycle dependent manner. (DNA is in blue)

The expression and activity of Aurora B are regulated according to the cell cycle. Expression of Aurora B reaches a maximum at the G2-M transition, whereas Aurora B protein is most active during mitosis.[6]

Aurora B is a chromosomal passenger protein. Specifically, Aurora B localizes to the chromosomes in prophase, the centromere in prometaphase and metaphase, and the central mitotic spindle in anaphase.[8] This localization has been determined by indirect immunofluorescence in mammalian, C. elegans, and Drosophila cells. A more detailed analysis of Aurora B localization has been carried out in mammalian cells by tagging Aurora B with green fluorescent protein.[9] This analysis showed that the association of Aurora B with centromeres is dynamic (Aurora B at the centromere is constantly exchanging with a pool of cytoplasmic Aurora B). The analysis of tagged Aurora B also suggested that it associates with spindle microtubules during anaphase of mitosis and this association significantly limits its mobility. Finally, a portion of the tagged Aurora B localized to the equatorial cell cortex, having been transported to this location by astral microtubules.

Regulation of Aurora B

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Aurora B complexes with three other proteins, Survivin, Borealin and INCENP. Each of the four components of the complex is required for the proper localization and function of the other three.[10] INCENP stimulates Aurora B kinase activity. Survivin might do the same.[11]

Localization of Aurora B to the centromere during prometaphase and metaphase requires phosphorylation of the mammalian kinetochore-specific histone-H3 variant centromere protein A (CENP-A).[12] CENP-A associates with the centromere and is necessary for assembly of the kinetochore. Phosphorylation of CENP-A at serine 7 by Aurora A kinase recruits Aurora B to the centromere.[13] Aurora B, itself, can also phosphorylate CENP-A at the same residue once it is recruited (see below).

Additionally, topoisomerase II has been implicated in the regulation of Aurora B localization and enzymatic activity.[14] This regulatory role may be directly associated with the role of topoisomerase II in disjoining sister chromatids prior to anaphase. In topoisomerase II-depleted cells, Aurora B and INCENP do not transfer to the central spindle in late mitosis. Instead, they remain tightly associated with the centromeres of non-disjoined sister chromatids. Also, cells deficient in topoisomerase II show significantly reduced Aurora B kinase activity. Inhibition of Aurora B due to loss of topoisomerase II seems to depend on BubR1 activity (see below).

Aurora B has been shown to bind to end-binding protein 1 (EB1), a protein that regulates microtubule dynamics.[15] Indirect immunofluorescence showed that Aurora B and EB1 colocalize during anaphase on the central spindle and in the midbody during cytokinesis. Intriguingly, EB1 overexpression enhances Aurora B kinase activity, at least in part because EB1 blocks the dephosphorylation/inactivation of Aurora B by protein phosphatase 2A.

Role in chromosome biorientation

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Studies in several organisms indicate that Aurora B oversees chromosome biorientation by ensuring that appropriate connections are made between spindle microtubules and kinetochores.

Inhibition of Aurora B function by RNA interference[16] or microinjection of blocking antibodies[17] impairs the alignment of chromosomes at the equator of the mitotic spindle. This process of alignment is referred to as chromosome congression. The reason for this defect is a subject of ongoing study. Aurora B inhibition may lead to an increase in the number of syntelic attachments (sister chromatid pairs in which both sister kinetochores are attached to microtubules radiating from the same spindle pole).[18] Intriguingly, expression of a dominant-negative and catalytically inactive form of Aurora B disrupted microtubule attachment to the kinetochore and prevented the association of dynein and centromere protein E (CENP-E) with kinetochores.

Numerous kinetochore targets of Aurora kinases have been determined in organisms ranging from yeast to man. Most notably, CENP-A is a target of Aurora B.[12] The phosphorylation of CENP-A by Aurora B reaches a maximum in prometaphase. In fact, Aurora A targets the same CENP-A phosphorylation site as Aurora B, and CENP-A phosphorylation by Aurora A is thought to precede that by Aurora B. Thus, a model has been proposed in which CENP-A phosphorylation by Aurora A recruits Aurora B to the centromere, the latter maintaining the phosphorylation state of CENP-A in a positive feedback loop. Mutation of this phosphorylation site in CENP-A also leads to defects in cytokinesis[citation needed].

Aurora B also interacts with mitotic centromere-associated kinesin (MCAK). Both Aurora B and MCAK localize to the inner centromere during prometaphase.[19] Aurora B has been shown to recruit MCAK to the centromere and directly phosphorylate MCAK on various residues.[20] Phosphorylation of MCAK by Aurora B limits the ability of MCAK to depolymerize microtubules. Importantly, inhibition of MCAK by a number of approaches leads to improper attachment of kinetochores to spindle microtubules.[21]

It has been hypothesized that tension generated by amphitelic attachment (biorientation; the attachment of sister kinetochores to opposite spindle poles) pulls sister kinetochores apart, thus disrupting the interaction of Aurora B at the innermost portion of the centromere with microtubule binding sites on the fibrous corona of the outermost centromere. Specifically, the tension generated by biorientation pulls MCAK outside of the area of Aurora B localization.[20] Thus, mitosis proceeds upon biorientation and dissociation of Aurora B from its substrates.

Role in chromosome condensation and chromosome cohesion

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Aurora B is responsible for phosphorylation of histone-H3 on serine 10 during mitosis.[22] This modification is conserved from yeast (where the kinase is known as Ipl1) to human. Notably, histone-H3 phosphorylation by Aurora B seems not to be responsible for chromatin condensation. Though Aurora B is enriched at centromeres, it localizes diffusely to all chromatin.

In Drosophila cells, Aurora B depletion disrupts chromosome structure and compaction.[23] In these cells, the condensin complex does not localize appropriately to the chromosomes. Similarly, in C. elegans, condensin activity is dependent on Aurora B in metaphase.[24] However, in Xenopus egg cell-free extracts, condensin binding and chromosome condensation occur normally even in the absence of Aurora B.[25] Likewise, after treating cells with an Aurora B enzyme inhibitor (Aurora B localization is not affected), the condensin complex localizes normally.

Aurora B localizes to the paired arms of homologous chromosomes in metaphase I of C. elegans meiosis, and perturbs microtubule dynamics in mitosis.[26] Release of this cohesion, which is dependent on Aurora B, is required for progression to anaphase I and segregation of homologous chromosomes.[27] In mitotic vertebrate B lymphocytes, the proper centromeric localization of a number of Aurora B binding partners requires cohesin.[28]

Role in cytokinesis

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The Aurora B complex is necessary for cytokinesis in vertebrates, C. elegans, Drosophila, and fission yeast.

In various cell types, overexpression of a catalytically inactive Aurora B prevents cytokinesis.[7] Disruption of cytokinesis can also arise from Aurora B mislocalization due to mutation of Aurora B binding partners.[29]

Aurora B targets a number of proteins that localize to the cleavage furrow, including the type-III intermediate filament proteins vimentin,[30] desmin, and glial fibrillary acidic protein (GFAP).[31] In general, phosphorylation destabilizes intermediate filaments. Therefore, it has been proposed that phosphorylation of intermediate filaments at the cleavage furrow destabilizes the filaments in preparation for cytokinesis.[31] In agreement with this hypothesis, mutation of Aurora B target sites in intermediate filament proteins leads to defects in filament deformation and prevents the final stage of cytokinesis.

Aurora B also phosphorylates myosin II regulatory light chain at the cleavage furrow. Inhibition of Aurora B activity prevents proper myosin II localization to the cleavage furrow and disrupts spindle midzone organization.[32]

Role in the spindle assembly checkpoint

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The spindle assembly checkpoint inhibits progression of mitosis from metaphase to anaphase until all sister chromatid pairs are bioriented.

Presence of Aurora B halts metaphase-to-anaphase transition until proper biorientation is achieved. This is demonstrated in Aurora B deficient cells, where inhibition of Aurora B by hesperadin causes the cell to progress from metaphase to anaphase even when there are misaligned chromosomes in the cell.[33][34]

Aurora B may be involved in the localization of MAD2 and BubR1, proteins that recognize correct chromosome attachment to spindle microtubules. Loss of Aurora B lowers the concentration of Mad2 and BubR1 at the kinetochores. In particular, Aurora B seems to be responsible for maintaining the localization of Mad2 and BubR1 to the kinetochore following their initial recruitment, which occurs independent of Aurora B.[35] Aurora B may be directly or indirectly involved in the hyper-phosphorylation of BubR1 seen in mitosis in wild-type cells.[36]

Interactions

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Aurora B kinase has been shown to interact with:

Role in cancer

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Abnormally elevated levels of Aurora B kinase cause unequal chromosomal separation during cell division, resulting in the formation of cells with abnormal numbers of chromosomes, which are both a cause and driver of cancer.

Inhibition of Aurora B kinase by BI811283 in cancer cells leads to the formation of cells with severely abnormal numbers of chromosomes (polyploid). Counterintuitively, inhibition of Aurora B kinase actually causes the polyploid cells formed to continue dividing however, because these cells have severe chromosomal abnormalities, they eventually stop dividing or undergo cell death.[44][45]

Role in axonal outgrowth and axon regeneration

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A novel function for Aurora B kinase has recently been reported in neurons. Following axotomy of cultured neurons, significant upregulation in Aurora B kinase gene expression was observed coinciding with regenerative axonal sprouting.[46] Furthermore, overexpression of Aurora B kinase results in accelerated axonal outgrowth of spinal motor neurons in developing zebrafish.[47]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000178999 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020897 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: AURKB aurora kinase B".
  6. ^ a b Bischoff JR, Anderson L, Zhu Y, Mossie K, Ng L, Souza B, et al. (1998). "A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers". The EMBO Journal. 17 (11): 3052–65. doi:10.1093/emboj/17.11.3052. PMC 1170645. PMID 9606188.
  7. ^ a b Terada Y, Tatsuka M, Suzuki F, Yasuda Y, Fujita S, Otsu M (1998). "AIM-1: A mammalian midbody-associated protein required for cytokinesis". The EMBO Journal. 17 (3): 667–76. doi:10.1093/emboj/17.3.667. PMC 1170416. PMID 9450992.
  8. ^ Adams RR, Carmena M, Earnshaw WC (2001). "Chromosomal passengers and the (aurora) ABCs of mitosis". Trends in Cell Biology. 11 (2): 49–54. doi:10.1016/s0962-8924(00)01880-8. PMID 11166196.
  9. ^ Murata-Hori M, Tatsuka M, Wang YL (2002). "Probing the dynamics and functions of aurora B kinase in living cells during mitosis and cytokinesis". Molecular Biology of the Cell. 13 (4): 1099–108. doi:10.1091/mbc.01-09-0467. PMC 102254. PMID 11950924.
  10. ^ Honda R, Körner R, Nigg EA (2003). "Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis". Molecular Biology of the Cell. 14 (8): 3325–41. doi:10.1091/mbc.E02-11-0769. PMC 181570. PMID 12925766.
  11. ^ Chen J, Jin S, Tahir SK, Zhang H, Liu X, Sarthy AV, et al. (2003). "Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells". Journal of Biological Chemistry. 278 (1): 486–90. doi:10.1074/jbc.M211119200. PMID 12419797.
  12. ^ a b Zeitlin SG, Shelby RD, Sullivan KF (2001). "CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis". The Journal of Cell Biology. 155 (7): 1147–57. doi:10.1083/jcb.200108125. PMC 2199334. PMID 11756469.
  13. ^ Kunitoku N, Sasayama T, Marumoto T, Zhang D, Honda S, Kobayashi O, et al. (2003). "CENP-A phosphorylation by Aurora-A in prophase is required for enrichment of Aurora-B at inner centromeres and for kinetochore function". Developmental Cell. 5 (6): 853–64. doi:10.1016/s1534-5807(03)00364-2. PMID 14667408.
  14. ^ Coelho PA, Queiroz-Machado J, Carmo AM, Moutinho-Pereira S, Maiato H, Sunkel CE (2008). "Dual role of topoisomerase II in centromere resolution and aurora B activity". PLOS Biology. 6 (8): e207. doi:10.1371/journal.pbio.0060207. PMC 2525683. PMID 18752348.
  15. ^ Sun L, Gao J, Dong X, Liu M, Li D, Shi X, et al. (2008). "EB1 promotes Aurora-B kinase activity through blocking its inactivation by protein phosphatase 2A". Proceedings of the National Academy of Sciences. 105 (20): 7153–8. Bibcode:2008PNAS..105.7153S. doi:10.1073/pnas.0710018105. PMC 2438220. PMID 18477699.
  16. ^ Adams RR, Maiato H, Earnshaw WC, Carmena M (2001). "Essential roles of Drosophila inner centromere protein (INCENP) and aurora B in histone H3 phosphorylation, metaphase chromosome alignment, kinetochore disjunction, and chromosome segregation". The Journal of Cell Biology. 153 (4): 865–80. doi:10.1083/jcb.153.4.865. PMC 2192373. PMID 11352945.
  17. ^ Kallio MJ, McCleland ML, Stukenberg PT, Gorbsky GJ (2002). "Inhibition of aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis". Current Biology. 12 (11): 900–5. Bibcode:2002CBio...12..900K. doi:10.1016/s0960-9822(02)00887-4. PMID 12062053. S2CID 13939857.
  18. ^ Hauf S, Cole RW, Laterra S, Zimmer C, Schnapp G, Walter R, et al. (2003). "The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint". The Journal of Cell Biology. 161 (2): 281–94. doi:10.1083/jcb.200208092. PMC 2172906. PMID 12707311.
  19. ^ Wordeman L, Wagenbach M, Maney T (1999). "Mutations in the ATP-binding domain affect the subcellular distribution of mitotic centromere-associated kinesin (MCAK)". Cell Biology International. 23 (4): 275–86. doi:10.1006/cbir.1999.0359. PMID 10600236. S2CID 29403722.
  20. ^ a b Andrews PD, Ovechkina Y, Morrice N, Wagenbach M, Duncan K, Wordeman L, et al. (2004). "Aurora B regulates MCAK at the mitotic centromere". Developmental Cell. 6 (2): 253–68. doi:10.1016/s1534-5807(04)00025-5. PMID 14960279.
  21. ^ Kline-Smith SL, Khodjakov A, Hergert P, Walczak CE (2004). "Depletion of centromeric MCAK leads to chromosome congression and segregation defects due to improper kinetochore attachments". Molecular Biology of the Cell. 15 (3): 1146–59. doi:10.1091/mbc.E03-08-0581. PMC 363095. PMID 14699064.
  22. ^ Hsu JY, Sun ZW, Li X, Reuben M, Tatchell K, Bishop DK, et al. (2000). "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes". Cell. 102 (3): 279–91. doi:10.1016/s0092-8674(00)00034-9. PMID 10975519. S2CID 16057773.
  23. ^ Giet R, Glover DM (2001). "Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis". The Journal of Cell Biology. 152 (4): 669–82. doi:10.1083/jcb.152.4.669. PMC 2195771. PMID 11266459.
  24. ^ Crosio C, Fimia GM, Loury R, Kimura M, Okano Y, Zhou H, et al. (2002). "Mitotic phosphorylation of histone H3: Spatio-temporal regulation by mammalian Aurora kinases". Molecular and Cellular Biology. 22 (3): 874–85. doi:10.1128/mcb.22.3.874-885.2002. PMC 133550. PMID 11784863.
  25. ^ MacCallum DE, Losada A, Kobayashi R, Hirano T (2002). "ISWI remodeling complexes in Xenopus egg extracts: Identification as major chromosomal components that are regulated by INCENP-aurora B". Molecular Biology of the Cell. 13 (1): 25–39. doi:10.1091/mbc.01-09-0441. PMC 65070. PMID 11809820.
  26. ^ Kaitna S, Pasierbek P, Jantsch M, Loidl J, Glotzer M (2002). "The aurora B kinase AIR-2 regulates kinetochores during mitosis and is required for separation of homologous Chromosomes during meiosis". Current Biology. 12 (10): 798–812. Bibcode:2002CBio...12..798K. doi:10.1016/s0960-9822(02)00820-5. PMID 12015116. S2CID 2215023.
  27. ^ Rogers E, Bishop JD, Waddle JA, Schumacher JM, Lin R (2002). "The aurora kinase AIR-2 functions in the release of chromosome cohesion in Caenorhabditis elegans meiosis". The Journal of Cell Biology. 157 (2): 219–29. doi:10.1083/jcb.200110045. PMC 1855215. PMID 11940606.
  28. ^ Sonoda E, Matsusaka T, Morrison C, Vagnarelli P, Hoshi O, Ushiki T, et al. (2001). "Scc1/Rad21/Mcd1 is required for sister chromatid cohesion and kinetochore function in vertebrate cells". Developmental Cell. 1 (6): 759–70. doi:10.1016/s1534-5807(01)00088-0. PMID 11740938.
  29. ^ MacKay AM, Ainsztein AM, Eckley DM, Earnshaw WC (1998). "A dominant mutant of inner centromere protein (INCENP), a chromosomal protein, disrupts prometaphase congression and cytokinesis". The Journal of Cell Biology. 140 (5): 991–1002. doi:10.1083/jcb.140.5.991. PMC 2132686. PMID 9490714.
  30. ^ Goto H, Yasui Y, Kawajiri A, Nigg EA, Terada Y, Tatsuka M, et al. (2003). "Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process". Journal of Biological Chemistry. 278 (10): 8526–30. doi:10.1074/jbc.M210892200. PMID 12458200.
  31. ^ a b Kawajiri A, Yasui Y, Goto H, Tatsuka M, Takahashi M, Nagata K, et al. (2003). "Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinatedly with Rho-kinase". Molecular Biology of the Cell. 14 (4): 1489–500. doi:10.1091/mbc.E02-09-0612. PMC 153117. PMID 12686604.
  32. ^ Murata-Hori M, Fumoto K, Fukuta Y, Iwasaki T, Kikuchi A, Tatsuka M, et al. (2000). "Myosin II regulatory light chain as a novel substrate for AIM-1, an aurora/Ipl1p-related kinase from rat". Journal of Biochemistry. 128 (6): 903–7. doi:10.1093/oxfordjournals.jbchem.a022840. PMID 11098131.
  33. ^ Hauf S, Cole RW, Laterra S, Zimmer C, Schnapp G, Walter R, et al. (2003). "The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint". The Journal of Cell Biology. 161 (2): 281–94. doi:10.1083/jcb.200208092. PMC 2172906. PMID 12707311.
  34. ^ Santaguida S, Vernieri C, Villa F, Ciliberto A, Musacchio A (2011-04-20). "Evidence that Aurora B is implicated in spindle checkpoint signalling independently of error correction". The EMBO Journal. 30 (8): 1508–1519. doi:10.1038/emboj.2011.70. ISSN 1460-2075. PMC 3102279. PMID 21407176.
  35. ^ Lens SM, Wolthuis RM, Klompmaker R, Kauw J, Agami R, Brummelkamp T, et al. (2003). "Survivin is required for a sustained spindle checkpoint arrest in response to lack of tension". The EMBO Journal. 22 (12): 2934–47. doi:10.1093/emboj/cdg307. PMC 162159. PMID 12805209.
  36. ^ Ditchfield C, Johnson VL, Tighe A, Ellston R, Haworth C, Johnson T, et al. (2003). "Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores". The Journal of Cell Biology. 161 (2): 267–80. doi:10.1083/jcb.200208091. PMC 2172902. PMID 12719470.
  37. ^ Ryser S, Dizin E, Jefford CE, Delaval B, Gagos S, Christodoulidou A, et al. (February 2009). "Distinct roles of BARD1 isoforms in mitosis: full-length BARD1 mediates Aurora B degradation, cancer-associated BARD1beta scaffolds Aurora B and BRCA2". Cancer Research. 69 (3): 1125–34. doi:10.1158/0008-5472.CAN-08-2134. PMID 19176389.
  38. ^ Wheatley SP, Carvalho A, Vagnarelli P, Earnshaw WC (June 2001). "INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis". Current Biology. 11 (11): 886–90. Bibcode:2001CBio...11..886W. doi:10.1016/S0960-9822(01)00238-X. PMID 11516652. S2CID 381637.
  39. ^ Chen J, Jin S, Tahir SK, Zhang H, Liu X, Sarthy AV, et al. (January 2003). "Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells". J. Biol. Chem. 278 (1): 486–90. doi:10.1074/jbc.M211119200. PMID 12419797.
  40. ^ Sampath SC, Ohi R, Leismann O, Salic A, Pozniakovski A, Funabiki H (July 2004). "The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly". Cell. 118 (2): 187–202. doi:10.1016/j.cell.2004.06.026. PMID 15260989. S2CID 17795816.
  41. ^ Gassmann R, Carvalho A, Henzing AJ, Ruchaud S, Hudson DF, Honda R, et al. (July 2004). "Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle". J. Cell Biol. 166 (2): 179–91. doi:10.1083/jcb.200404001. PMC 2172304. PMID 15249581.
  42. ^ Delaval B, Ferrand A, Conte N, Larroque C, Hernandez-Verdun D, Prigent C, et al. (June 2004). "Aurora B -TACC1 protein complex in cytokinesis". Oncogene. 23 (26): 4516–22. doi:10.1038/sj.onc.1207593. PMID 15064709.
  43. ^ Chen BB, Glasser JR, Coon TA, Mallampalli RK (August 2013). "Skp-cullin-F box E3 ligase component FBXL2 ubiquitinates Aurora B to inhibit tumorigenesis". Cell Death & Disease. 4 (8): e759. doi:10.1038/cddis.2013.271. ISSN 2041-4889. PMC 3763433. PMID 23928698.
  44. ^ Gürtler U, Tontsch-Grunt U, Jarvis M, Zahn SK, Boehmelt G, Quant J, et al. (2010). "Effect of BI 811283, a novel inhibitor of Aurora B kinase, on tumor senescence and apoptosis". J. Clin. Oncol. 28 (15 Suppl e13632): e13632. doi:10.1200/jco.2010.28.15_suppl.e13632.
  45. ^ Sorrentino R, Libertini S, Pallante PL, Troncone G, Palombini L, Bavetsias V, et al. (2005). "Aurora B overexpression associates with the thyroid carcinoma undifferentiated phenotype and is required for thyroid carcinoma cell proliferation". J. Clin. Endocrinol. Metab. 90 (2): 928–35. doi:10.1210/jc.2004-1518. PMID 15562011.
  46. ^ Ng JM, Chen MJ, Leung JY, Peng ZF, Manikandan J, Qi RZ, et al. (Apr 2012). "Transcriptional insights on the regenerative mechanics of axotomized neurons in vitro". Journal of Cellular and Molecular Medicine. 16 (4): 789–811. doi:10.1111/j.1582-4934.2011.01361.x. PMC 3822849. PMID 21711447.
  47. ^ Gwee SS, Radford RA, Chow S, Syal MD, Morsch M, Formella I, et al. (Dec 2017). "Aurora kinase B regulates axonal outgrowth and regeneration in the spinal motor neurons of developing zebrafish". Cellular and Molecular Life Sciences. 75 (23): 4269–4285. doi:10.1007/s00018-018-2780-5. PMC 11105541. PMID 29468257. S2CID 3408586.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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