オーロラBキナーゼとは？ わかりやすく解説

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オーロラBキナーゼ

(オーロラB から転送)

出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2023/08/13 15:01 UTC 版)

オーロラBキナーゼまたはオーロラキナーゼB（オーロラB、英: Aurora kinase B、Aurora B）は、ヒトではAURKB遺伝子にコードされるタンパク質であり、紡錘体の中心体への接着過程に機能する。


出典
  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:
  4. ^ Mouse PubMed Reference:
  5. ^ “Entrez Gene: AURKB aurora kinase B”. 2023年8月7日閲覧。
  6. ^ a b Bischoff, J. R.; Anderson, L; Zhu, Y; Mossie, K; Ng, L; Souza, B; Schryver, B; Flanagan, P 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170645/. 
  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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170416/. 
  8. ^ Adams, R. R.; Carmena, M; Earnshaw, W. C. (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, Y. L. (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC102254/. 
  10. ^ Honda, R; Körner, R; Nigg, E. A. (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC181570/. 
  11. ^ Chen, J; Jin, S; Tahir, S. K.; Zhang, H; Liu, X; Sarthy, A. V.; McGonigal, T. P.; Liu, Z 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, S. G.; Shelby, R. D.; Sullivan, K. F. (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2199334/. 
  13. ^ Kunitoku, N; Sasayama, T; Marumoto, T; Zhang, D; Honda, S; Kobayashi, O; Hatakeyama, K; Ushio, Y 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, P. A.; Queiroz-Machado, J; Carmo, A. M.; Moutinho-Pereira, S; Maiato, H; Sunkel, C. E. (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2525683/. 
  15. ^ Sun, L; Gao, J; Dong, X; Liu, M; Li, D; Shi, X; Dong, J. T.; Lu, 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2438220/. 
  16. ^ Adams, R. R.; Maiato, H; Earnshaw, W. C.; 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192373/. 
  17. ^ Kallio, M. J.; McCleland, M. L.; Stukenberg, P. T.; Gorbsky, G. J. (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. doi:10.1016/s0960-9822(02)00887-4. PMID 12062053. 
  18. ^ Hauf, S; Cole, R. W.; Laterra, S; Zimmer, C; Schnapp, G; Walter, R; Heckel, A; Van Meel, J 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172906/. 
  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. 
  20. ^ a b Andrews, P. D.; Ovechkina, Y; Morrice, N; Wagenbach, M; Duncan, K; Wordeman, L; Swedlow, J. R. (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, S. L.; Khodjakov, A; Hergert, P; Walczak, C. E. (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC363095/. 
  22. ^ Hsu, J. Y.; Sun, Z. W.; Li, X; Reuben, M; Tatchell, K; Bishop, D. K.; Grushcow, J. M.; Brame, C. J. 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. 
  23. ^ Giet, R; Glover, D. M. (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195771/. 
  24. ^ Crosio, C; Fimia, G. M.; Loury, R; Kimura, M; Okano, Y; Zhou, H; Sen, S; Allis, C. D. 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC133550/. 
  25. ^ MacCallum, D. E.; 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC65070/. 
  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. doi:10.1016/s0960-9822(02)00820-5. PMID 12015116. 
  27. ^ Rogers, E; Bishop, J. D.; Waddle, J. A.; Schumacher, J. M.; 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1855215/. 
  28. ^ Sonoda, E; Matsusaka, T; Morrison, C; Vagnarelli, P; Hoshi, O; Ushiki, T; Nojima, K; Fukagawa, 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, A. M.; Ainsztein, A. M.; Eckley, D. M.; Earnshaw, W. C. (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132686/. 
  30. ^ Goto, H; Yasui, Y; Kawajiri, A; Nigg, E. A.; Terada, Y; Tatsuka, M; Nagata, K; Inagaki, M (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; Inagaki, M (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC153117/. 
  32. ^ Murata-Hori, M; Fumoto, K; Fukuta, Y; Iwasaki, T; Kikuchi, A; Tatsuka, M; Hosoya, H (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, R. W.; Laterra, S; Zimmer, C; Schnapp, G; Walter, R; Heckel, A; Van Meel, J 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172906/. 
  34. ^ Santaguida, Stefano; Vernieri, Claudio; Villa, Fabrizio; Ciliberto, Andrea; Musacchio, Andrea (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3102279/. 
  35. ^ Lens, S. M.; Wolthuis, R. M.; Klompmaker, R; Kauw, J; Agami, R; Brummelkamp, T; Kops, G; Medema, R. H. (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC162159/. 
  36. ^ Ditchfield, C; Johnson, V. L.; Tighe, A; Ellston, R; Haworth, C; Johnson, T; Mortlock, A; Keen, N 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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172902/. 
  37. ^ “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. (February 2009). doi:10.1158/0008-5472.CAN-08-2134. PMID 19176389. 
  38. ^ “INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis”. Current Biology 11 (11): 886–90. (June 2001). doi:10.1016/S0960-9822(01)00238-X. PMID 11516652. 
  39. ^ “Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells”. J. Biol. Chem. 278 (1): 486–90. (January 2003). doi:10.1074/jbc.M211119200. PMID 12419797. 
  40. ^ “The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly”. Cell 118 (2): 187–202. (July 2004). doi:10.1016/j.cell.2004.06.026. PMID 15260989. 
  41. ^ “Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle”. J. Cell Biol. 166 (2): 179–91. (July 2004). doi:10.1083/jcb.200404001. PMC 2172304. PMID 15249581. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172304/. 
  42. ^ “Aurora B -TACC1 protein complex in cytokinesis”. Oncogene 23 (26): 4516–22. (June 2004). doi:10.1038/sj.onc.1207593. PMID 15064709. 
  43. ^ Chen, B B; Glasser, J R; Coon, T A; Mallampalli, R K (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. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3763433/. 
  44. ^ “Effect of BI 811283, a novel inhibitor of Aurora B kinase, on tumor senescence and apoptosis”. J. Clin. Oncol. 28 (15 Suppl e13632): e13632. (2010). doi:10.1200/jco.2010.28.15_suppl.e13632. 
  45. ^ “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. (2005). doi:10.1210/jc.2004-1518. PMID 15562011. 
  46. ^ “Transcriptional insights on the regenerative mechanics of axotomized neurons in vitro.”. Journal of Cellular and Molecular Medicine 16 (4): 789–811. (Apr 2012). doi:10.1111/j.1582-4934.2011.01361.x. PMC 3822849. PMID 21711447. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3822849/. 
  47. ^ “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. (Dec 2017). doi:10.1007/s00018-018-2780-5. PMID 29468257. 

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オーロラBキナーゼのお隣キーワード

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